Publications
1994
Dimarcq Jean-Luc, Hoffmann Danièle, Meister Marie, Bulet Philippe, Lanot R, Reichhart Jean-Marc, Hoffmann Jules A
Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity Journal Article
In: Eur. J. Biochem., vol. 221, no. 1, pp. 201–209, 1994, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription
@article{dimarcq_characterization_1994,
title = {Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity},
author = {Jean-Luc Dimarcq and Danièle Hoffmann and Marie Meister and Philippe Bulet and R Lanot and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0014-2956},
year = {1994},
date = {1994-04-01},
journal = {Eur. J. Biochem.},
volume = {221},
number = {1},
pages = {201--209},
abstract = {Insect defensins are a family of 4-kDa, cationic, inducible antibacterial peptides which bear six cysteine residues engaged in three intramolecular disulfide bridges. They owe their name to certain sequence similarities with defensins from mammalian neutrophiles and macrophages. We report the characterization of a novel defensin isoform from Drosophila and the cloning of the gene encoding a preprodefensin. The gene, which is intronless and present in a single copy/haploid genome, maps at position 46CD on the right arm of the second chromosome. The analysis of the upstream region of the gene reveals the presence of multiple putative cis-regulatory sequences similar to mammalian regulatory motifs of acute-phase-response genes. Transcriptional profiles indicate that the Drosophila defensin gene is induced by bacterial challenge with acute-phase kinetics. It is also expressed in the absence of immune challenge during metamorphosis. These and other data on the Drosophila defensin gene lead us to suggest that insect and mammalian defensins have evolved independently.},
keywords = {Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription},
pubstate = {published},
tppubtype = {article}
}
Moine H., Dahlberg A. E.
Mutations in helix 34 of Escherichia coli 16 S ribosomal RNA have multiple effects on ribosome function and synthesis Journal Article
In: J Mol Biol, vol. 243, no. 3, pp. 402-12, 1994, (0022-2836 Journal Article).
Abstract | BibTeX | Tags: *Mutation, *Nucleic, *Translation, &, 16S/*chemistry/genetics, Acid, Base, beta-Galactosidase/genetics, Codon, coli/*genetics/growth, Conformation, Data, development, Escherichia, Genetic, Gov't, Molecular, Non-U.S., P.H.S., Ribosomal, Ribosomes/*metabolism, RNA, Sequence, Support, Terminator, U.S.
@article{,
title = {Mutations in helix 34 of Escherichia coli 16 S ribosomal RNA have multiple effects on ribosome function and synthesis},
author = { H. Moine and A. E. Dahlberg},
year = {1994},
date = {1994-01-01},
journal = {J Mol Biol},
volume = {243},
number = {3},
pages = {402-12},
abstract = {Helix 34 of E. coli 16 S rRNA (1046 to 1067 and 1189 to 1211) has been proposed to participate directly in the termination of translation at UGA stop codons. We have constructed mutations in this helix in plasmid-encoded rDNA to explore the specific functional roles of the sequence UCAUCA (1199 to 1204) and a secondary structure also involving positions 1054 and 1057-1058. The rRNA mutations were analyzed for their effects on in vivo translational accuracy (stop codon readthrough and frameshifting) as well as growth rate, ribosome synthesis and incorporation into polysomes. Mutations at positions 1054, 1057, 1058, 1199 and 1200 had significant effects on translational accuracy, causing non-specific readthrough of all three stop codons as well as enhanced +1 and -1 frameshifting. Mutations at 1202 and 1203, however, had no effect. The incorporation of deleterious mutant subunits into 70 S ribosomes and polysomes was severely reduced and was associated with a slower growth rate and increased synthesis of host-encoded ribosomes. These data support the proposal that helix 34 is an essential component of the decoding center of the 30 S ribosomal subunit and is not restricted in function to UGA-codon specific termination.},
note = {0022-2836
Journal Article},
keywords = {*Mutation, *Nucleic, *Translation, &, 16S/*chemistry/genetics, Acid, Base, beta-Galactosidase/genetics, Codon, coli/*genetics/growth, Conformation, Data, development, Escherichia, Genetic, Gov't, Molecular, Non-U.S., P.H.S., Ribosomal, Ribosomes/*metabolism, RNA, Sequence, Support, Terminator, U.S.},
pubstate = {published},
tppubtype = {article}
}
Santos M. A., el-Adlouni C., Cox A. D., Luz J. M., Keith G., Tuite M. F.
Transfer RNA profiling: a new method for the identification of pathogenic Candida species Journal Article
In: Yeast, vol. 10, no. 5, pp. 625-36, 1994, (0749-503x Journal Article).
Abstract | BibTeX | Tags: Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis
@article{,
title = {Transfer RNA profiling: a new method for the identification of pathogenic Candida species},
author = { M. A. Santos and C. el-Adlouni and A. D. Cox and J. M. Luz and G. Keith and M. F. Tuite},
year = {1994},
date = {1994-01-01},
journal = {Yeast},
volume = {10},
number = {5},
pages = {625-36},
abstract = {A new molecular taxonomic method applicable to the identification of medically important Candida species and other yeast species has been developed. It is based on the electrophoretic pattern of total tRNA samples (a 'tRNA profile') isolated from Candida species and generated using high-resolution semi-denaturing urea-polyacrylamide gel electrophoresis and methylene blue staining. Species-specific tRNA profiles for the species C. albicans, C. tropicalis, C. parapsilosis, C. guilliermondii, C. glabrata and Pichia guilliermondii were obtained. Detailed studies with the major human pathogen of the Candida genus, C. albicans, demonstrated that the tRNA profile for a given species was both reproducible and strain-independent; seven different C. albicans strains generated identical tRNA profiles. Minor strain-specific heterogeneities in the tRNA profiles of C. guilliermondii and C. parapsilosis were detected, but in neither case did they significantly alter the species-specific diagnostic tRNA profile. The potential of this method in clarifying taxonomic anomalies was demonstrated by the finding that Type I and Type II strains of C. stellatoidea generate very different tRNA profiles, with that of a Type II strain being identical to the C. albicans tRNA profile. This method offers a number of advantages over current electrophoretic karyotype methods for species identification, both within the Candida genus and with yeast species in general.},
note = {0749-503x
Journal Article},
keywords = {Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis},
pubstate = {published},
tppubtype = {article}
}
Wilhelm M., Wilhelm F. X., Keith G., Agoutin B., Heyman T.
Yeast Ty1 retrotransposon: the minus-strand primer binding site and a cis-acting domain of the Ty1 RNA are both important for packaging of primer tRNA inside virus-like particles Journal Article
In: Nucleic Acids Res, vol. 22, no. 22, pp. 4560-5, 1994, (0305-1048 Journal Article).
Abstract | BibTeX | Tags: Acid, Amino, Base, Binding, cerevisiae/*genetics, Cloning, Data, Fungal/*genetics, Genetic, Gov't, Met/*genetics, Molecular, Mutation/physiology, Non-U.S., Retroelements/*genetics/physiology, Retroviridae/genetics, RNA, RNA/*genetics, Saccharomyces, Sequence, Sites, Support, Transcription, Transfer
@article{,
title = {Yeast Ty1 retrotransposon: the minus-strand primer binding site and a cis-acting domain of the Ty1 RNA are both important for packaging of primer tRNA inside virus-like particles},
author = { M. Wilhelm and F. X. Wilhelm and G. Keith and B. Agoutin and T. Heyman},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {22},
pages = {4560-5},
abstract = {Reverse transcription of the yeast retrotransposon Ty1 is primed by the cytoplasmic initiator methionine tRNA (tRNA(iMet)). The primer tRNA(iMet) is packaged inside virus-like particles (VLPs) and binds to a 10 nucleotides minus-strand primer binding site, the (-)PBS, complementary to its 3' acceptor stem. We have found that three short sequences of the Ty1 RNA (box 1, box 2.1 and box 2.2) located 3' to the (-)PBS are complementary to other regions of the primer tRNA(iMet) (T psi C and DHU stems and loops). Reconstitution of reverse transcription in vitro with T7 transcribed Ty1 RNA species and tRNA(iMet) purified from yeast cells shows that the boxes do not affect the efficiency of reverse transcription. Thus the role of the boxes on packaging of the primer tRNA(iMet) into the VLPs was investigated by analysing the level of tRNA(iMet) packaged into mutant VLPs. Specific nucleotide changes in the (-)PBS or in the boxes that do not change the protein coding sequence but disrupt the complementarity with the primer tRNA(iMet) within the VLPs. We propose that base pairing between the primer tRNA(iMet) and the Ty1 RNA is of major importance for tRNA(iMet) packaging into the VLPs. Moreover the intactness of the boxes is essential for retrotransposition as shown by the transposition defect of a Ty1 element harboring an intact (-)PBS and mutated boxes.},
note = {0305-1048
Journal Article},
keywords = {Acid, Amino, Base, Binding, cerevisiae/*genetics, Cloning, Data, Fungal/*genetics, Genetic, Gov't, Met/*genetics, Molecular, Mutation/physiology, Non-U.S., Retroelements/*genetics/physiology, Retroviridae/genetics, RNA, RNA/*genetics, Saccharomyces, Sequence, Sites, Support, Transcription, Transfer},
pubstate = {published},
tppubtype = {article}
}
Wilhelm M, Wilhelm F X, Keith G, Agoutin B, Heyman T
In: Nucleic Acids Res, vol. 22, no. 22, pp. 4560-4565, 1994, ISBN: 7527135, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Sequence Base Sequence Binding Sites Cloning, Fungal/*genetics RNA, Genetic, Met/*genetics Retroelements/*genetics/physiology Retroviridae/genetics Saccharomyces cerevisiae/*genetics Support, Molecular Molecular Sequence Data Mutation/physiology RNA/*genetics RNA, Non-U.S. Gov't Transcription, Transfer, Unité ARN
@article{,
title = {Yeast Ty1 retrotransposon: the minus-strand primer binding site and a cis-acting domain of the Ty1 RNA are both important for packaging of primer tRNA inside virus-like particles},
author = {M Wilhelm and F X Wilhelm and G Keith and B Agoutin and T Heyman},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7527135},
isbn = {7527135},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {22},
pages = {4560-4565},
abstract = {Reverse transcription of the yeast retrotransposon Ty1 is primed by the cytoplasmic initiator methionine tRNA (tRNA(iMet)). The primer tRNA(iMet) is packaged inside virus-like particles (VLPs) and binds to a 10 nucleotides minus-strand primer binding site, the (-)PBS, complementary to its 3' acceptor stem. We have found that three short sequences of the Ty1 RNA (box 1, box 2.1 and box 2.2) located 3' to the (-)PBS are complementary to other regions of the primer tRNA(iMet) (T psi C and DHU stems and loops). Reconstitution of reverse transcription in vitro with T7 transcribed Ty1 RNA species and tRNA(iMet) purified from yeast cells shows that the boxes do not affect the efficiency of reverse transcription. Thus the role of the boxes on packaging of the primer tRNA(iMet) into the VLPs was investigated by analysing the level of tRNA(iMet) packaged into mutant VLPs. Specific nucleotide changes in the (-)PBS or in the boxes that do not change the protein coding sequence but disrupt the complementarity with the primer tRNA(iMet) within the VLPs. We propose that base pairing between the primer tRNA(iMet) and the Ty1 RNA is of major importance for tRNA(iMet) packaging into the VLPs. Moreover the intactness of the boxes is essential for retrotransposition as shown by the transposition defect of a Ty1 element harboring an intact (-)PBS and mutated boxes.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid Sequence Base Sequence Binding Sites Cloning, Fungal/*genetics RNA, Genetic, Met/*genetics Retroelements/*genetics/physiology Retroviridae/genetics Saccharomyces cerevisiae/*genetics Support, Molecular Molecular Sequence Data Mutation/physiology RNA/*genetics RNA, Non-U.S. Gov't Transcription, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Vysotskaya V, Tischenko S, Garber M, Kern D, Mougel M, Ehresmann C, Ehresmann B
In: Eur J Biochem, vol. 223, no. 2, pp. 437-445, 1994, ISBN: 7519982, (0014-2956 Journal Article).
Abstract | Links | BibTeX | Tags: 16S/*metabolism Recombinant Proteins/metabolism Ribosomal Proteins/chemistry/*genetics/isolation & purification/metabolism Sequence Alignment Support, Amino Acid Sequence Base Sequence Blotting, Bacterial Molecular Sequence Data Molecular Weight Nucleic Acid Hybridization Polymerase Chain Reaction Promoter Regions (Genetics) Protein Binding Protein Structure, Bacterial/chemistry/genetics/isolation & purification Escherichia coli/genetics/metabolism *Gene Expression *Genes, Bacterial/metabolism RNA, Genetic, Molecular DNA, Non-U.S. Gov't Thermus thermophilus/*genetics Transcription, Ribosomal, Secondary RNA, Southern Cloning, Unité ARN
@article{,
title = {The ribosomal protein S8 from Thermus thermophilus VK1. Sequencing of the gene, overexpression of the protein in Escherichia coli and interaction with rRNA},
author = {V Vysotskaya and S Tischenko and M Garber and D Kern and M Mougel and C Ehresmann and B Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7519982},
isbn = {7519982},
year = {1994},
date = {1994-01-01},
journal = {Eur J Biochem},
volume = {223},
number = {2},
pages = {437-445},
abstract = {The gene of the ribosomal protein S8 from Thermus thermophilus VK1 has been isolated from a genomic library by hybridization of an oligonucleotide coding for the N-terminal amino acid sequence of the protein, amplified by PCR and sequenced. Nucleotide sequence reveals an open reading frame coding for a protein of 138 amino acid residues (M(r) 15,839). The codon usage shows that 94% of the codons possess G or C in the third position, and agrees with the preferential usage of codons of high G+C content in the bacteria of the genus Thermus. The amino acid sequence of the protein shows 48% identity with the protein from Escherichia coli. Ribosomal protein S8 from T. thermophilus has been expressed in E. coli under the control of the T7 promoter and purified to homogeneity by heat treatment of the extract followed by cation-exchange chromatography. Conditions were defined in which T. thermophilus protein S8 binds specifically an homologous 16S rRNA fragment containing the putative S8 binding site with an apparent association constant of 5 x 10(7) M-1. The overexpressed protein binds the rRNA with the same affinity as that extracted from T. thermophilus, indicating that the thermophilic protein is correctly folded in E. coli. The specificity of this binding is dependent on the ionic strength. The protein S8 from T. thermophilus recognizes the E. coli rRNA binding sites as efficiently as the S8 protein from E. coli. This result agrees with sequence comparisons of the S8 binding site on the small subunit rRNA from E. coli and from T. thermophilus, showing strong similarities in the regions involved in the interaction. It suggests that the structural features responsible for the recognition are conserved in the mesophilic and thermophilic eubacteria, despite structural peculiarities in the thermophilic partners conferring thermostability.},
note = {0014-2956
Journal Article},
keywords = {16S/*metabolism Recombinant Proteins/metabolism Ribosomal Proteins/chemistry/*genetics/isolation & purification/metabolism Sequence Alignment Support, Amino Acid Sequence Base Sequence Blotting, Bacterial Molecular Sequence Data Molecular Weight Nucleic Acid Hybridization Polymerase Chain Reaction Promoter Regions (Genetics) Protein Binding Protein Structure, Bacterial/chemistry/genetics/isolation & purification Escherichia coli/genetics/metabolism *Gene Expression *Genes, Bacterial/metabolism RNA, Genetic, Molecular DNA, Non-U.S. Gov't Thermus thermophilus/*genetics Transcription, Ribosomal, Secondary RNA, Southern Cloning, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Philippe C, Benard L, Eyermann F, Cachia C, Kirillov S V, Portier C, Ehresmann B, Ehresmann C
Structural elements of rps0 mRNA involved in the modulation of translational initiation and regulation of E. coli ribosomal protein S15 Journal Article
In: Nucleic Acids Res, vol. 22, no. 13, pp. 2538-2546, 1994, ISBN: 8041615, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence Cloning, Genetic, Messenger/*chemistry/metabolism RNA, Molecular Escherichia coli/*genetics Kinetics Lac Operon Molecular Sequence Data Mutation Nucleic Acid Conformation Operon Protein Binding RNA, Non-U.S. Gov't *Translation, Ribosomal/metabolism Ribosomal Proteins/*genetics Support, Unité ARN
@article{,
title = {Structural elements of rps0 mRNA involved in the modulation of translational initiation and regulation of E. coli ribosomal protein S15},
author = {C Philippe and L Benard and F Eyermann and C Cachia and S V Kirillov and C Portier and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8041615},
isbn = {8041615},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {13},
pages = {2538-2546},
abstract = {Previous experiments showed that S15 inhibits its own translation by binding to its mRNA in a region overlapping the ribosome loading site. This binding was postulated to stabilize a pseudoknot structure that exists in equilibrium with two stem-loops and to trap the ribosome on its mRNA loading site in a transitory state. In this study, we investigated the effect of mutations in the translational operator on: the binding of protein S15, the formation of the 30S/mRNA/tRNA(fMet) ternary initiation complex, the ability of S15 to inhibit the formation of this ternary complex. The results were compared to in vivo expression and repression rates. The results show that (1) the pseudoknot is required for S15 recognition and translational control; (2) mRNA and 16S rRNA efficiently compete for S15 binding and 16S rRNA suppresses the ability of S15 to inhibit the formation of the active ternary complex; (3) the ribosome binds more efficiently to the pseudoknot than to the stem-loop; (4) sequences located between nucleotides 12 to 47 of the S15 coding phase enhances the efficiency of ribosome binding in vitro; this is correlated with enhanced in vivo expression and regulation rates.},
note = {0305-1048
Journal Article},
keywords = {Base Sequence Cloning, Genetic, Messenger/*chemistry/metabolism RNA, Molecular Escherichia coli/*genetics Kinetics Lac Operon Molecular Sequence Data Mutation Nucleic Acid Conformation Operon Protein Binding RNA, Non-U.S. Gov't *Translation, Ribosomal/metabolism Ribosomal Proteins/*genetics Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Lutz Y, Eberhard D, Jacq X, Krol A, Grummt I, Davidson I, Chambon P, Tora L
The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters Journal Article
In: EMBO J, vol. 13, no. 5, pp. 1166-1175, 1994, ISBN: 7510635, (0261-4189 Journal Article).
Abstract | Links | BibTeX | Tags: Antibodies, Genetic, LESCURE, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors/biosynthesis/isolation & purification/*metabolism *Transcription, Unité ARN
@article{,
title = {The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters},
author = {A Lescure and Y Lutz and D Eberhard and X Jacq and A Krol and I Grummt and I Davidson and P Chambon and L Tora},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7510635},
isbn = {7510635},
year = {1994},
date = {1994-01-01},
journal = {EMBO J},
volume = {13},
number = {5},
pages = {1166-1175},
abstract = {In eukaryotes, the TATA box binding protein (TBP) is an integral component of the transcription initiation complexes of all three classes of nuclear RNA polymerases. In this study we have investigated the role of the N-terminal region of human TBP in transcription initiation from RNA polymerase (Pol) I, II and III promoters by using three monoclonal antibodies (mAbs). Each antibody recognizes a distinct epitope in the N-terminal domain of human TBP. We demonstrate that these antibodies differentially affect transcription from distinct classes of promoters. One antibody, mAb1C2, and a synthetic peptide comprising its epitope selectively inhibited in vitro transcription from TATA-containing, but not from TATA-less promoters, irrespective of whether they were transcribed by Pol II or Pol III. Transcription by Pol I, on the other hand, was not affected. Two other antibodies and their respective epitope peptides did not affect transcription from any of the promoters tested. Order of addition experiments indicate that mAb1C2 did not prevent binding of TBP to the TATA box or the formation of the TBP-TFIIA-TFIIB complex but rather inhibited a subsequent step of preinitiation complex formation. These data suggest that a defined region within the N-terminal domain of human TBP may be involved in specific protein-protein interactions required for the assembly of functional preinitiation complexes on TATA-containing, but not on TATA-less promoters.},
note = {0261-4189
Journal Article},
keywords = {Antibodies, Genetic, LESCURE, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors/biosynthesis/isolation & purification/*metabolism *Transcription, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Blomberg P, Engdahl H M, Malmgren C, Romby P, Wagner E G
In: Mol Microbiol, vol. 12, no. 1, pp. 49-60, 1994, ISBN: 7520116, (0950-382x Journal Article).
Abstract | Links | BibTeX | Tags: Antisense/chemistry/*physiology RNA, Bacterial Models, Bacterial Proteins/genetics/*metabolism Base Sequence Binding Sites *DNA Replication *Gene Expression Regulation, Bacterial/*genetics Reading Frames Ribosomes/*metabolism Sequence Alignment Support, Genetic, Genetic Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Peptides/*genetics/physiology *Proteins R Factors/*genetics RNA, Non-U.S. Gov't Translation, ROMBY, Unité ARN
@article{,
title = {Replication control of plasmid R1: disruption of an inhibitory RNA structure that sequesters the repA ribosome-binding site permits tap-independent RepA synthesis},
author = {P Blomberg and H M Engdahl and C Malmgren and P Romby and E G Wagner},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7520116},
isbn = {7520116},
year = {1994},
date = {1994-01-01},
journal = {Mol Microbiol},
volume = {12},
number = {1},
pages = {49-60},
abstract = {The replication frequency of plasmid R1 is controlled by an antisense RNA, CopA, that inhibits the synthesis of the replication initiator protein, RepA, at the post-transcriptional level. This inhibition is indirect and affects translation of a leader peptide reading frame (tap). Translation of tap is required for repA translation (Blomberg et al., 1992). Here we asked whether an RNA stem-loop sequestering the repA ribosome-binding site blocks tap translation-independent repA expression. Destabilization of this structure resulted in tap-independent RepA synthesis, concomitant with a loss of CopA-mediated inhibition; thus, CopA acts at the level of tap translation. Structure probing of RepA mRNAs confirmed that the introduced mutations induced a local destabilization in the repA ribosome-binding site stem-loop. An increased spacing between the repA Shine-Dalgarno region and the start codon permitted even higher repA expression. In Incl alpha/IncB plasmids, an RNA pseudoknot acts as an activator for rep translation. We suggest that the regulatory pathway in plasmid R1 does not involve an activator RNA pseudoknot.},
note = {0950-382x
Journal Article},
keywords = {Antisense/chemistry/*physiology RNA, Bacterial Models, Bacterial Proteins/genetics/*metabolism Base Sequence Binding Sites *DNA Replication *Gene Expression Regulation, Bacterial/*genetics Reading Frames Ribosomes/*metabolism Sequence Alignment Support, Genetic, Genetic Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Peptides/*genetics/physiology *Proteins R Factors/*genetics RNA, Non-U.S. Gov't Translation, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1993
Georgel Philippe, Meister Marie, Kappler Christine, Lemaitre Bruno, Reichhart Jean-Marc, Hoffmann Jules A
Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements Journal Article
In: Biochem. Biophys. Res. Commun., vol. 197, no. 2, pp. 508–517, 1993, ISSN: 0006-291X.
Abstract | Links | BibTeX | Tags: Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart
@article{georgel_insect_1993,
title = {Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements},
author = {Philippe Georgel and Marie Meister and Christine Kappler and Bruno Lemaitre and Jean-Marc Reichhart and Jules A Hoffmann},
doi = {10.1006/bbrc.1993.2508},
issn = {0006-291X},
year = {1993},
date = {1993-12-01},
journal = {Biochem. Biophys. Res. Commun.},
volume = {197},
number = {2},
pages = {508--517},
abstract = {We are using the diptericin gene as a model system to study the control of expression of the genes encoding antibacterial peptides during the Drosophila immune reaction. In order to investigate the putative regulatory regions in the diptericin promoter, we performed DNaseI footprinting experiments combined with gel-shift assays in two inducible systems: the larval fat body and a tumorous Drosophila blood cell line. Our results confirm the importance of kappa B-like elements previously described in the immune response of insects and reveal for the first time the involvement of other regions containing sequences homologous to mammalian acute-phase response elements.},
keywords = {Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart},
pubstate = {published},
tppubtype = {article}
}
Kappler Christine, Meister Marie, Lagueux Marie, Gateff E, Hoffmann Jules A, Reichhart Jean-Marc
Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila Journal Article
In: EMBO J., vol. 12, no. 4, pp. 1561–1568, 1993, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection
@article{kappler_insect_1993,
title = {Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila},
author = {Christine Kappler and Marie Meister and Marie Lagueux and E Gateff and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {1993},
date = {1993-04-01},
journal = {EMBO J.},
volume = {12},
number = {4},
pages = {1561--1568},
abstract = {The Drosophila diptericin gene codes for a 9 kDa antibacterial peptide and is rapidly and transiently expressed in larvae and adults after bacterial challenge. It is also induced in a tumorous Drosophila blood cell line by the addition of lipopolysaccharide (LPS). The promoter of this gene contains two 17 bp repeats located closely upstream of the TATA-box and harbouring a decameric kappa B-related sequence. This study reports that the replacement of the two 17 bp repeats by random sequences abolishes bacteria inducibility in transgenic fly lines. In transfected tumorous blood cells, the replacement of both or either of the 17 bp motifs reduces dramatically LPS inducibility, whereas multiple copies significantly increase the level of transcriptional activation by LPS challenge. A specific DNA-protein binding activity is evidenced in cytoplasmic and nuclear extracts of induced blood cells and fat body. It is absent in controls. It is proposed that induction of the diptericin gene mediated by the two 17 bp repeats occurs via a mechanism similar to that of mammalian NF-kappa B.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection},
pubstate = {published},
tppubtype = {article}
}
Pfeiffer P., Jung J. L., Heitzler J., Keith G.
Unusual structure of the double-stranded RNA associated with the '447' cytoplasmic male sterility in Vicia faba Journal Article
In: J Gen Virol, vol. 74, no. Pt 6, pp. 1167-73, 1993, (0022-1317 Journal Article).
Abstract | BibTeX | Tags: *Plants, &, Base, Bodies, Cytoplasm, Data, Extrachromosomal, Fabaceae/*genetics, Genetic, Inclusion, Infertility/genetics, Inheritance/*genetics, Medicinal, Molecular, Pollen/genetics, purification, Replicase/metabolism, RNA, RNA/*genetics/isolation, Sequence, Transcription, Viral
@article{,
title = {Unusual structure of the double-stranded RNA associated with the '447' cytoplasmic male sterility in Vicia faba},
author = { P. Pfeiffer and J. L. Jung and J. Heitzler and G. Keith},
year = {1993},
date = {1993-01-01},
journal = {J Gen Virol},
volume = {74},
number = {Pt 6},
pages = {1167-73},
abstract = {The 16.7 kbp dsRNA specific to the '447' cytoplasmic male sterility (CMS) line of Vicia faba was labelled in vitro with [alpha-32P]ATP and poly(A) polymerase, and by T4 RNA ligase-mediated addition of [32P]pCp. Analysis of the reaction products under denaturing conditions revealed in both cases extensive labelling of a 4.5 kb ssRNA, already detected in previous experiments in which the RNA-dependent RNA polymerase associated with the dsRNA was allowed to pursue RNA synthesis on preinitiated complexes. Mobility shift analysis of total pCp-labelled dsRNA revealed not two but three different 3' termini. The most prominent sequencing pattern corresponded to the 4.5 kb ssRNA, indicating that this RNA species has a preferentially accessible, free 3' OH extremity. Northern blot analysis of the denatured dsRNA confirmed that the 4.5 kb ssRNA is a subgenomic mRNA and detected its counterpart of about 12 kb. Nearly all 16.7 kbp dsRNA molecules featured an interrupted positive-sense strand, indicating a marked prevalence of transcription over replication complexes. This unusual strategy of transcription by a strand displacement mechanism, following initiation at an internal discontinuity, is compared with that of other dsRNA viruses or defective viruses, and is discussed in relation to the expression of the CMS trait.},
note = {0022-1317
Journal Article},
keywords = {*Plants, &, Base, Bodies, Cytoplasm, Data, Extrachromosomal, Fabaceae/*genetics, Genetic, Inclusion, Infertility/genetics, Inheritance/*genetics, Medicinal, Molecular, Pollen/genetics, purification, Replicase/metabolism, RNA, RNA/*genetics/isolation, Sequence, Transcription, Viral},
pubstate = {published},
tppubtype = {article}
}
Santos M. A., Keith G., Tuite M. F.
Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon Journal Article
In: EMBO J, vol. 12, no. 2, pp. 607-16, 1993, (0261-4189 Journal Article).
Abstract | BibTeX | Tags: *Anticodon, *Translation, &, Acid, albicans/*genetics, Base, Candida, Cloning, Conformation, Data, DNA, Fungal, Fungal/chemistry/genetics/isolation, Genes, Genetic, Gov't, Leucine/*genetics, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, Ser/chemistry/*genetics/isolation, Support, Transfer
@article{,
title = {Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon},
author = { M. A. Santos and G. Keith and M. F. Tuite},
year = {1993},
date = {1993-01-01},
journal = {EMBO J},
volume = {12},
number = {2},
pages = {607-16},
abstract = {From in vitro translation studies we have previously demonstrated the existence of an apparent efficient UAG (amber) suppressor tRNA in the dimorphic fungus Candida albicans (Santos et al., 1990). Using an in vitro assay for termination codon readthrough the tRNA responsible was purified to homogeneity from C.albicans cells. The determined sequence of the purified tRNA predicts a 5'-CAG-3' anticodon that should decode the leucine codon CUG and not the UAG termination codon as originally hypothesized. However, the tRNA(CAG) sequence shows greater nucleotide homology with seryl-tRNAs from the closely related yeast Saccharomyces cerevisiae than with leucyl-tRNAs from the same species. In vitro tRNA-charging studies demonstrated that the purified tRNA(CAG) is charged with Ser. The gene encoding the tRNA was cloned from C.albicans by a PCR-based strategy and DNA sequence analysis confirmed both the structure of the tRNA(CAG) and the absence of any introns in the tRNA gene. The copy number of the tRNA(CAG) gene (1-2 genes per haploid genome) is in agreement with the relatively low abundance (< 0.5% total tRNA) of this tRNA. In vitro translation studies revealed that the purified tRNA(CAG) could induce apparent translational bypass of all three termination codons. However, peptide mapping of in vitro translation products demonstrated that the tRNA(CAG) induces translational misreading in the amino-terminal region of two RNA templates employed, namely the rabbit alpha- and beta-globin mRNAs. These results suggest that the C.albicans tRNA(CAG) is not an 'omnipotent' suppressor tRNA but rather may mediate a novel non-standard translational event in vitro during the translation of the CUG codon. The possible nature of this non-standard translation event is discussed in the context of both the unusual structural features of the tRNA(CAG) and its in vitro behaviour.},
note = {0261-4189
Journal Article},
keywords = {*Anticodon, *Translation, &, Acid, albicans/*genetics, Base, Candida, Cloning, Conformation, Data, DNA, Fungal, Fungal/chemistry/genetics/isolation, Genes, Genetic, Gov't, Leucine/*genetics, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, Ser/chemistry/*genetics/isolation, Support, Transfer},
pubstate = {published},
tppubtype = {article}
}
Reichhart Jean-Marc, Georgel Philippe, Meister Marie, Lemaitre Bruno, Kappler Christine, Hoffmann Jules A
Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila Journal Article
In: C. R. Acad. Sci. III, Sci. Vie, vol. 316, no. 10, pp. 1218–1224, 1993, ISSN: 0764-4469.
Abstract | BibTeX | Tags: Animals, Blotting, Cellular, Gene Expression, Genes, Genetic, hoffmann, Immunity, Insect, M3i, NF-kappa B, Northern, reichhart, translocation, Zygote
@article{reichhart_expression_1993,
title = {Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila},
author = {Jean-Marc Reichhart and Philippe Georgel and Marie Meister and Bruno Lemaitre and Christine Kappler and Jules A Hoffmann},
issn = {0764-4469},
year = {1993},
date = {1993-01-01},
journal = {C. R. Acad. Sci. III, Sci. Vie},
volume = {316},
number = {10},
pages = {1218--1224},
abstract = {The rel/NF-kappa B-related morphogen dorsal is a maternally expressed gene which is involved in the control of the dorso-ventral axis during early embryogenesis of Drosophila. We show that this gene is also expressed in the fat body of larvae and adults of Drosophila as well as in a tumorous blood cell line: its expression is noticeably enhanced upon bacterial (or lipopolysaccharide) challenge. This challenge also induces within 15-30 min a nuclear translocation of the dorsal protein. The genes encoding inducible antibacterial peptides in Drosophila contain kappa B-related nucleotide sequences and we show that the dorsal protein can bind to such motifs and sequence-specifically transactivate a reporter gene in co-transfection experiments with a Drosophila cell line. However, in dl1 mutants, in the absence of dorsal protein, the genes encoding antibacterial peptides retain their inducibility, suggesting a multifactorial control. The results indicate that in addition to its role in embryogenesis, dorsal is involved in the immune response of Drosophila. They also strengthen the analogy between the mammalian acute phase response and the insect immune response.},
keywords = {Animals, Blotting, Cellular, Gene Expression, Genes, Genetic, hoffmann, Immunity, Insect, M3i, NF-kappa B, Northern, reichhart, translocation, Zygote},
pubstate = {published},
tppubtype = {article}
}
Santos M A, Keith G, Tuite M F
Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon Journal Article
In: EMBO J, vol. 12, no. 2, pp. 607-616, 1993, ISBN: 8440250, (0261-4189 Journal Article).
Abstract | Links | BibTeX | Tags: *Anticodon Base Sequence Candida albicans/*genetics Cloning, Fungal Genes, Fungal Leucine/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Fungal/chemistry/genetics/isolation & purification RNA, Genetic, Molecular DNA, Non-U.S. Gov't *Translation, Ser/chemistry/*genetics/isolation & purification Support, Transfer, Unité ARN
@article{,
title = {Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon},
author = {M A Santos and G Keith and M F Tuite},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8440250},
isbn = {8440250},
year = {1993},
date = {1993-01-01},
journal = {EMBO J},
volume = {12},
number = {2},
pages = {607-616},
abstract = {From in vitro translation studies we have previously demonstrated the existence of an apparent efficient UAG (amber) suppressor tRNA in the dimorphic fungus Candida albicans (Santos et al., 1990). Using an in vitro assay for termination codon readthrough the tRNA responsible was purified to homogeneity from C.albicans cells. The determined sequence of the purified tRNA predicts a 5'-CAG-3' anticodon that should decode the leucine codon CUG and not the UAG termination codon as originally hypothesized. However, the tRNA(CAG) sequence shows greater nucleotide homology with seryl-tRNAs from the closely related yeast Saccharomyces cerevisiae than with leucyl-tRNAs from the same species. In vitro tRNA-charging studies demonstrated that the purified tRNA(CAG) is charged with Ser. The gene encoding the tRNA was cloned from C.albicans by a PCR-based strategy and DNA sequence analysis confirmed both the structure of the tRNA(CAG) and the absence of any introns in the tRNA gene. The copy number of the tRNA(CAG) gene (1-2 genes per haploid genome) is in agreement with the relatively low abundance (< 0.5% total tRNA) of this tRNA. In vitro translation studies revealed that the purified tRNA(CAG) could induce apparent translational bypass of all three termination codons. However, peptide mapping of in vitro translation products demonstrated that the tRNA(CAG) induces translational misreading in the amino-terminal region of two RNA templates employed, namely the rabbit alpha- and beta-globin mRNAs. These results suggest that the C.albicans tRNA(CAG) is not an 'omnipotent' suppressor tRNA but rather may mediate a novel non-standard translational event in vitro during the translation of the CUG codon. The possible nature of this non-standard translation event is discussed in the context of both the unusual structural features of the tRNA(CAG) and its in vitro behaviour.},
note = {0261-4189
Journal Article},
keywords = {*Anticodon Base Sequence Candida albicans/*genetics Cloning, Fungal Genes, Fungal Leucine/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Fungal/chemistry/genetics/isolation & purification RNA, Genetic, Molecular DNA, Non-U.S. Gov't *Translation, Ser/chemistry/*genetics/isolation & purification Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Podyminogin M A, Vlassov V V, Giege R
Synthetic RNA-cleaving molecules mimicking ribonuclease A active center. Design and cleavage of tRNA transcripts Journal Article
In: Nucleic Acids Res, vol. 21, no. 25, pp. 5950-5956, 1993, ISBN: 7507235, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Asp/*metabolism Ribonuclease, Base Sequence Binding Sites Hydrogen-Ion Concentration Molecular Sequence Data Nucleic Acid Conformation RNA/metabolism RNA, Genetic, Non-U.S. Gov't Temperature Transcription, Pancreatic/antagonists & inhibitors/chemical synthesis/*metabolism Substrate Specificity Support, Transfer, Unité ARN
@article{,
title = {Synthetic RNA-cleaving molecules mimicking ribonuclease A active center. Design and cleavage of tRNA transcripts},
author = {M A Podyminogin and V V Vlassov and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7507235},
isbn = {7507235},
year = {1993},
date = {1993-01-01},
journal = {Nucleic Acids Res},
volume = {21},
number = {25},
pages = {5950-5956},
abstract = {RNA cleaving molecules were synthesized by conjugating imidazole residues imitating the essential imidazoles in the active center of pancreatic ribonuclease to an intercalating compound, derivative of phenazine capable of binding to the double stranded regions of polynucleotides. Action of the molecules on tRNA was investigated. It was found, that some of the compounds bearing two imidazole residues cleave tRNA under physiological conditions. The cleavage reaction shows a bell-shaped pH dependence with a maximum at pH 7.0 indicating participation of protonated and non-protonated imidazole residues in the process. Under the conditions stabilizing the tRNA structure, a tRNAAsp transcript was cleaved preferentially at the junctions of the stem and loop regions of the cloverleaf tRNA fold, at the five positions C56, C43, C20.1, U13, and U8, with a marked preference for C56. This cleavage pattern is consistent with a hydrolysis mechanism involving non-covalent binding of the compounds to the double-stranded regions of tRNA followed by an attack of the imidazole residues at the juxtaposed flexible single-stranded regions of the molecule. The compounds provide new probes for the investigation of RNA structure in solution and potential reactive groups for antisense oligonucleotide derivatives.},
note = {0305-1048
Journal Article},
keywords = {Asp/*metabolism Ribonuclease, Base Sequence Binding Sites Hydrogen-Ion Concentration Molecular Sequence Data Nucleic Acid Conformation RNA/metabolism RNA, Genetic, Non-U.S. Gov't Temperature Transcription, Pancreatic/antagonists & inhibitors/chemical synthesis/*metabolism Substrate Specificity Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Pfeiffer P, Jung J L, Heitzler J, Keith G
Unusual structure of the double-stranded RNA associated with the '447' cytoplasmic male sterility in Vicia faba Journal Article
In: J Gen Virol, vol. 74, no. Pt 6, pp. 1167-1173, 1993, ISBN: 7685375, (0022-1317 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence Cytoplasm Extrachromosomal Inheritance/*genetics Fabaceae/*genetics Inclusion Bodies, Genetic, Medicinal Pollen/genetics RNA/*genetics/isolation & purification RNA Replicase/metabolism Transcription, Unité ARN, Viral Infertility/genetics Molecular Sequence Data *Plants
@article{,
title = {Unusual structure of the double-stranded RNA associated with the '447' cytoplasmic male sterility in Vicia faba},
author = {P Pfeiffer and J L Jung and J Heitzler and G Keith},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7685375},
isbn = {7685375},
year = {1993},
date = {1993-01-01},
journal = {J Gen Virol},
volume = {74},
number = {Pt 6},
pages = {1167-1173},
abstract = {The 16.7 kbp dsRNA specific to the '447' cytoplasmic male sterility (CMS) line of Vicia faba was labelled in vitro with [alpha-32P]ATP and poly(A) polymerase, and by T4 RNA ligase-mediated addition of [32P]pCp. Analysis of the reaction products under denaturing conditions revealed in both cases extensive labelling of a 4.5 kb ssRNA, already detected in previous experiments in which the RNA-dependent RNA polymerase associated with the dsRNA was allowed to pursue RNA synthesis on preinitiated complexes. Mobility shift analysis of total pCp-labelled dsRNA revealed not two but three different 3' termini. The most prominent sequencing pattern corresponded to the 4.5 kb ssRNA, indicating that this RNA species has a preferentially accessible, free 3' OH extremity. Northern blot analysis of the denatured dsRNA confirmed that the 4.5 kb ssRNA is a subgenomic mRNA and detected its counterpart of about 12 kb. Nearly all 16.7 kbp dsRNA molecules featured an interrupted positive-sense strand, indicating a marked prevalence of transcription over replication complexes. This unusual strategy of transcription by a strand displacement mechanism, following initiation at an internal discontinuity, is compared with that of other dsRNA viruses or defective viruses, and is discussed in relation to the expression of the CMS trait.},
note = {0022-1317
Journal Article},
keywords = {Base Sequence Cytoplasm Extrachromosomal Inheritance/*genetics Fabaceae/*genetics Inclusion Bodies, Genetic, Medicinal Pollen/genetics RNA/*genetics/isolation & purification RNA Replicase/metabolism Transcription, Unité ARN, Viral Infertility/genetics Molecular Sequence Data *Plants},
pubstate = {published},
tppubtype = {article}
}
Isel C, Marquet R, Keith G, Ehresmann C, Ehresmann B
Modified nucleotides of tRNA(3Lys) modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription Journal Article
In: J Biol Chem, vol. 268, no. 34, pp. 25269-25272, 1993, ISBN: 7503978, (0021-9258 Journal Article).
Abstract | Links | BibTeX | Tags: Anticodon/genetics/metabolism Base Sequence Binding Sites Comparative Study DNA Primers HIV-1/genetics/*metabolism HIV-1 Reverse Transcriptase HIV-2/genetics/metabolism Molecular Sequence Data Nucleic Acid Conformation RNA, Genetic, Genetic *Transcription, Lys/*metabolism RNA, MARQUET, Non-U.S. Gov't Templates, Transfer, Unité ARN, Viral/*biosynthesis RNA-Directed DNA Polymerase/*metabolism SIV/genetics/metabolism Support
@article{,
title = {Modified nucleotides of tRNA(3Lys) modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription},
author = {C Isel and R Marquet and G Keith and C Ehresmann and B Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7503978},
isbn = {7503978},
year = {1993},
date = {1993-01-01},
journal = {J Biol Chem},
volume = {268},
number = {34},
pages = {25269-25272},
abstract = {In all retroviruses, reverse transcription is primed by a tRNA whose 3' end 18 nucleotides are complementary to the so called viral primer binding site. Previous work showed that reverse transcription of HIV-1 RNA is initiated by tRNA(3Lys). Using a variety of chemical and enzymatic structural probes, we investigated the interactions between HIV-1 RNA and its natural primer tRNA(3Lys). In addition to the predictable contacts between the viral primer binding site and the 3' end of tRNA(3Lys), a specific interaction takes place between an A-rich loop located upstream of the primer binding site region and the anticodon loop of tRNA(3Lys). This AAAA/Umcm5s2UUU loop-loop interaction is not observed when the natural primer is replaced by an in vitro synthesized tRNA(3Lys) transcript. Furthermore, dethiolation of the modified nucleotide mcm5s2U at position 34 of tRNA(3Lys) strongly destabilizes this interaction. Sequence and structure comparisons indicate that the primer/template loop-loop interaction is conserved in all HIV-1 isolates, and possibly also in HIV-2 and SIV.},
note = {0021-9258
Journal Article},
keywords = {Anticodon/genetics/metabolism Base Sequence Binding Sites Comparative Study DNA Primers HIV-1/genetics/*metabolism HIV-1 Reverse Transcriptase HIV-2/genetics/metabolism Molecular Sequence Data Nucleic Acid Conformation RNA, Genetic, Genetic *Transcription, Lys/*metabolism RNA, MARQUET, Non-U.S. Gov't Templates, Transfer, Unité ARN, Viral/*biosynthesis RNA-Directed DNA Polymerase/*metabolism SIV/genetics/metabolism Support},
pubstate = {published},
tppubtype = {article}
}
Brunel C, Romby P, Moine H, Caillet J, Grunberg-Manago M, Springer M, Ehresmann B, Ehresmann C
In: Biochimie, vol. 75, no. 12, pp. 1167-1179, 1993, ISBN: 8199252, (0300-9084 Journal Article).
Abstract | Links | BibTeX | Tags: Bacterial/*genetics Molecular Sequence Data Mutation Nucleic Acid Conformation *Operator Regions (Genetics) Point Mutation Protein Structure, Base Sequence Escherichia coli/*enzymology/genetics Gene Deletion Gene Expression Regulation, Genetic, Messenger/chemistry/metabolism RNA, Met/chemistry/metabolism Ribosomes/metabolism Structure-Activity Relationship Support, Non-U.S. Gov't Threonine-tRNA Ligase/chemistry/*genetics/metabolism Translation, ROMBY, Secondary RNA, Transfer, Unité ARN
@article{,
title = {Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains},
author = {C Brunel and P Romby and H Moine and J Caillet and M Grunberg-Manago and M Springer and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8199252},
isbn = {8199252},
year = {1993},
date = {1993-01-01},
journal = {Biochimie},
volume = {75},
number = {12},
pages = {1167-1179},
abstract = {Previous work showed that E coli threonyl-tRNA synthetase (ThrRS) binds to the leader region of its own mRNA and represses its translation by blocking ribosome binding. The operator consists of four distinct domains, one of them (domain 2) sharing structural analogies with the anticodon arm of the E coli tRNA(Thr). The regulation specificity can be switched by using tRNA identity rules, suggesting that the operator could be recognized by ThrRS as a tRNA-like structure. In the present paper, we investigated the relative contribution of the four domains to the regulation process by using deletions and point mutations. This was achieved by testing the effects of the mutations on RNA conformation (by probing experiments), on ThrRS recognition (by footprinting experiments and measure of the competition with tRNA(Thr) for aminoacylation), on ribosome binding and ribosome/ThrRS competition (by toeprinting experiments). It turns out that: i) the four domains are structurally and functionally independent; ii) domain 2 is essential for regulation and contains the major structural determinants for ThrRS binding; iii) domain 4 is involved in control and ThrRS recognition, but to a lesser degree than domain 2. However, the previously described analogies with the acceptor-like stem are not functionally significant. How it is recognized by ThrRS remains to be resolved; iv) domain 1, which contains the ribosome loading site, is not involved in ThrRS recognition. The binding of ThrRS probably masks the ribosome binding site by steric hindrance and not by direct contacts. This is only achieved when ThrRS interacts with both domains 2 and 4; and v) the unpaired domain 3, which connects domains 2 and 4, is not directly involved in ThrRS recognition. It should serve as an articulation to provide an appropriate spacing between domains 2 and 4. Furthermore, it is possibly involved in ribosome binding.},
note = {0300-9084
Journal Article},
keywords = {Bacterial/*genetics Molecular Sequence Data Mutation Nucleic Acid Conformation *Operator Regions (Genetics) Point Mutation Protein Structure, Base Sequence Escherichia coli/*enzymology/genetics Gene Deletion Gene Expression Regulation, Genetic, Messenger/chemistry/metabolism RNA, Met/chemistry/metabolism Ribosomes/metabolism Structure-Activity Relationship Support, Non-U.S. Gov't Threonine-tRNA Ligase/chemistry/*genetics/metabolism Translation, ROMBY, Secondary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Baudin F, Marquet R, Isel C, Darlix J L, Ehresmann B, Ehresmann C
Functional sites in the 5' region of human immunodeficiency virus type 1 RNA form defined structural domains Journal Article
In: J Mol Biol, vol. 229, no. 2, pp. 382-397, 1993, ISBN: 8429553, (0022-2836 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence Electrophoresis, Genetic, MARQUET, Non-U.S. Gov't Translation, Polyacrylamide Gel HIV-1/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Unité ARN, Viral/*chemistry/metabolism Rabbits Support
@article{,
title = {Functional sites in the 5' region of human immunodeficiency virus type 1 RNA form defined structural domains},
author = {F Baudin and R Marquet and C Isel and J L Darlix and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8429553},
isbn = {8429553},
year = {1993},
date = {1993-01-01},
journal = {J Mol Biol},
volume = {229},
number = {2},
pages = {382-397},
abstract = {The 5' region of HIV-1 RNA contains functional elements involved in key steps of the retroviral cycle, such as genomic RNA transcription, splicing, translation, dimerization or initiation of reverse transcription. In the present work, we investigated the conformation of the first 500 nucleotides covering the RNA leader and the 5' gag coding sequences of HIV-MAL, using chemical probing. We provide detailed information on almost each nucleotide at one of their Watson-Crick positions and on position N-7 of purines. Experiments were conducted on two in vitro transcribed RNA fragments (1 to 707 and 1 to 311). A secondary structure model was derived by combining the experimental data, computer predictions and sequence comparison. Under conditions favoring dimerization (high salt concentration), HIV-1 RNA folds into independent structural domains that can be related to defined functional regions. The first domain corresponds to TAR forming a stable stem-loop. Intrinsic structural features are found to stabilize the TAR hairpin loop. The second domain (nucleotides 56 to 299) contains the PBS sequence, which is located in a stable subdomain constrained by a four stem junction (nucleotides 139 to 218). Although the MAL isolate has an insertion near the PBS, probably resulting from the duplication of a 23-nucleotide sequence, the structural organization of this subdomain is conserved in all other HIV-1 isolates. The third domain (nucleotides 300 to 404) contains the splice donor site, packaging and dimerization elements and the AUG initiation codon of gag. A major result is the structural versatility of this region. Two mutually exclusive structures, both equally in agreement with probing data, could modulate the different functions involving this domain. The reduced accessibility of the gag translational initiation site possibly accounts for the low efficiency of the in vitro translation of the dimer. Finally, the 5' gag coding sequences form a metastable domain.},
note = {0022-2836
Journal Article},
keywords = {Animals Base Sequence Electrophoresis, Genetic, MARQUET, Non-U.S. Gov't Translation, Polyacrylamide Gel HIV-1/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Unité ARN, Viral/*chemistry/metabolism Rabbits Support},
pubstate = {published},
tppubtype = {article}
}
1992
Reichhart Jean-Marc, Meister Marie, Dimarcq Jean-Luc, Zachary Daniel, Hoffmann Danièle, Ruiz C, Richards G, Hoffmann Jules A
Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter Journal Article
In: EMBO J., vol. 11, no. 4, pp. 1469–1477, 1992, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Acute-Phase Proteins, Adipose Tissue, Animals, Base Sequence, beta-Galactosidase, Embryo, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Mammals, Nonmammalian, Oligodeoxyribonucleotides, Promoter Regions, Recombinant Fusion Proteins, reichhart, Restriction Mapping
@article{reichhart_insect_1992,
title = {Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter},
author = {Jean-Marc Reichhart and Marie Meister and Jean-Luc Dimarcq and Daniel Zachary and Danièle Hoffmann and C Ruiz and G Richards and Jules A Hoffmann},
issn = {0261-4189},
year = {1992},
date = {1992-01-01},
journal = {EMBO J.},
volume = {11},
number = {4},
pages = {1469--1477},
abstract = {Diptericins are 9 kDa inducible antibacterial peptides initially isolated from immune haemolymph of Phormia (Diptera). Following the isolation of a Drosophila cDNA encoding a diptericin homologue, we have now cloned a genomic fragment containing the Drosophila diptericin gene. To dissect the regulation of this gene, we have transformed flies with a fusion gene in which the reporter beta-galactosidase gene is under the control of 2.2 kb upstream sequences of the diptericin gene. We show that such a fusion gene is inducible by injection of live bacteria or complete Freund's adjuvant and respects the tissue specific expression pattern of the resident diptericin gene. Our analysis reveals at least four distinct phases in the regulation of this gene: young larvae, late third instar larvae, pupae and adults. This complexity may be related to the presence in the upstream sequences of multiple copies of response elements previously characterized in genes encoding acute phase response proteins in mammals (e.g. NK-kappa B, NF-kappa B related, NF-IL6 response elements).},
keywords = {Acute-Phase Proteins, Adipose Tissue, Animals, Base Sequence, beta-Galactosidase, Embryo, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Mammals, Nonmammalian, Oligodeoxyribonucleotides, Promoter Regions, Recombinant Fusion Proteins, reichhart, Restriction Mapping},
pubstate = {published},
tppubtype = {article}
}
Senger B, Despons L, Walter P, Fasiolo F
The anticodon triplet is not sufficient to confer methionine acceptance to a transfer RNA Journal Article
In: Proc Natl Acad Sci U S A, vol. 89, no. 22, pp. 10768-10771, 1992, ISBN: 1438273, (0027-8424 Journal Article).
Abstract | Links | BibTeX | Tags: Anticodon/genetics/*metabolism Base Sequence Kinetics Methionine/*metabolism Models, Genetic, Met/genetics/*metabolism Saccharomyces cerevisiae/*genetics Support, Non-U.S. Gov't Transcription, Structural Molecular Sequence Data Nucleic Acid Conformation RNA, Transfer, Unité ARN
@article{,
title = {The anticodon triplet is not sufficient to confer methionine acceptance to a transfer RNA},
author = {B Senger and L Despons and P Walter and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1438273},
isbn = {1438273},
year = {1992},
date = {1992-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {89},
number = {22},
pages = {10768-10771},
abstract = {Previous work suggested that the presence of the anticodon CAU alone was enough to confer methionine acceptance to a tRNA. Conversions of Escherichia coli nonmethionine tRNAs to a methionine-accepting species were obtained by substitutions reconstructing the whole methionine anticodon loop together with preservation (or introduction) of the acceptor stem base A73. We show here that the CAU triplet alone is unable to confer methionine acceptance when transplanted into a yeast aspartic tRNA. Both non-anticodon bases of the anticodon loop of yeast tRNA(Met) and A73 are required in addition to CAU for methionine acceptance. The importance of these non-anticodon bases in other CAU-containing tRNA frameworks was also established. These specific non-anticodon base interactions make a substantial thermodynamic contribution to the methionine acceptance of a transfer RNA.},
note = {0027-8424
Journal Article},
keywords = {Anticodon/genetics/*metabolism Base Sequence Kinetics Methionine/*metabolism Models, Genetic, Met/genetics/*metabolism Saccharomyces cerevisiae/*genetics Support, Non-U.S. Gov't Transcription, Structural Molecular Sequence Data Nucleic Acid Conformation RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Romby P, Brunel C, Caillet J, Springer M, Grunberg-Manago M, Westhof E, Ehresmann C, Ehresmann B
In: Nucleic Acids Res, vol. 20, no. 21, pp. 5633-5640, 1992, ISBN: 1280807, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Acylation Anticodon Base Sequence Binding, Bacterial Methionine-tRNA Ligase/metabolism Molecular Sequence Data Mutation Nucleic Acid Conformation *Operator Regions (Genetics) RNA, Bacterial/metabolism RNA, Competitive Escherichia coli/enzymology/*genetics *Gene Expression Regulation, Genetic, Met/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/antagonists & inhibitors/*genetics/metabolism Translation, ROMBY, Thr/metabolism Repressor Proteins/*metabolism Ribosomes/metabolism Support, Transfer, Transfer/*metabolism RNA, Unité ARN
@article{,
title = {Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules},
author = {P Romby and C Brunel and J Caillet and M Springer and M Grunberg-Manago and E Westhof and C Ehresmann and B Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1280807},
isbn = {1280807},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {21},
pages = {5633-5640},
abstract = {We previously showed that: (i) E.coli threonyl-tRNA synthetase (ThrRS) binds to the leader of its mRNA and represses translation by preventing ribosome binding to its loading site; (ii) the translational operator shares sequence and structure similarities with tRNA(Thr); (iii) it is possible to switch the specificity of the translational control from ThrRS to methionyl-tRNA synthetase (MetRS) by changing the CGU anticodon-like sequence to CAU, the tRNA(Met) anticodon. Here, we show that the wild type (CGU) and the mutated (CAU) operators act as competitive inhibitors of tRNA(Thr) and tRNA(fMet) for aminoacylation catalyzed by E.coli ThrRS and MetRS, respectively. The apparent Kd of the MetRS/CAU operator complex is one order magnitude higher than that of the ThrRS/CGU operator complex. Although ThrRS and MetRS shield the anticodon- and acceptor-like domains of their respective operators, the relative contribution of these two domains differs significantly. As in the threonine system, the interaction of MetRS with the CAU operator occludes ribosome binding to its loading site. The present data demonstrate that the anticodon-like sequence is one major determinant for the identity of the operator and the regulation specificity. It further shows that the tRNA-like operator obeys to tRNA identity rules.},
note = {0305-1048
Journal Article},
keywords = {Acylation Anticodon Base Sequence Binding, Bacterial Methionine-tRNA Ligase/metabolism Molecular Sequence Data Mutation Nucleic Acid Conformation *Operator Regions (Genetics) RNA, Bacterial/metabolism RNA, Competitive Escherichia coli/enzymology/*genetics *Gene Expression Regulation, Genetic, Met/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/antagonists & inhibitors/*genetics/metabolism Translation, ROMBY, Thr/metabolism Repressor Proteins/*metabolism Ribosomes/metabolism Support, Transfer, Transfer/*metabolism RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Graffe M, Dondon J, Caillet J, Romby P, Ehresmann C, Ehresmann B, Springer M
The specificity of translational control switched with transfer RNA identity rules Journal Article
In: Science, vol. 255, no. 5047, pp. 994-996, 1992, ISBN: 1372129, (0036-8075 Journal Article).
Abstract | Links | BibTeX | Tags: Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN
@article{,
title = {The specificity of translational control switched with transfer RNA identity rules},
author = {M Graffe and J Dondon and J Caillet and P Romby and C Ehresmann and B Ehresmann and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1372129},
isbn = {1372129},
year = {1992},
date = {1992-01-01},
journal = {Science},
volume = {255},
number = {5047},
pages = {994-996},
abstract = {The interaction of Escherichia coli threonyl-transfer RNA (tRNA) synthetase with the leader sequence of its own messenger RNA inhibits ribosome binding, resulting in negative translational feedback regulation. The leader sequence resembles the substrate (tRNA(Thr)) of the enzyme, and the nucleotides that mediate the correct recognition of the leader and the tRNA may be the same. A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to tRNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNA synthetase. This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs.},
note = {0036-8075
Journal Article},
keywords = {Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1991
Hipskind R A, Rao V N, Mueller C G, Reddy E S, Nordheim A
Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF Journal Article
In: Nature, vol. 354, no. 6354, pp. 531–534, 1991, ISSN: 0028-0836.
Abstract | Links | BibTeX | Tags: Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection
@article{hipskind_ets-related_1991,
title = {Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF},
author = {R A Hipskind and V N Rao and C G Mueller and E S Reddy and A Nordheim},
doi = {10.1038/354531a0},
issn = {0028-0836},
year = {1991},
date = {1991-12-01},
journal = {Nature},
volume = {354},
number = {6354},
pages = {531--534},
abstract = {A key event in the response of cells to proliferative signals is the rapid, transient induction of the c-fos proto-oncogene, which is mediated through the serum response element (SRE) in the fos promoter. Genomic footprinting and transfection experiments suggest that this activation occurs through a ternary complex that includes the serum response factor (SRF) and the ternary complex factor p62. Interaction of p62TCF with the SRF-SRE binary complex requires a CAGGA tract immediately upstream of the SRE. Proteins of the ets proto-oncogene family bind to similar sequences and we have found that a member of this family, Elk-1, forms SRF-dependent ternary complexes with the SRE. Elk-1 and p62TCF have the same DNA sequence requirements and antibodies against Elk-1 block the binding of both proteins. Furthermore, we show that like p62TCF, Elk-1 forms complexes with the yeast SRF-homologue MCM1 but not with yeast ARG80. But ARG80 mutants that convey interaction with p62TCF can also form complexes with Elk-1. The similarity, or even identity, between Elk-1 and p62TCF suggests a novel regulatory role for Ets proteins that is effected through interaction with other proteins, such as SRF. Furthermore, the possible involvement of an Ets protein in the control of c-fos has interesting implications for proto-oncogene cooperation in cellular growth control.},
keywords = {Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection},
pubstate = {published},
tppubtype = {article}
}
1990
Hoffmann Jules A, Hoffmann Danièle
The inducible antibacterial peptides of dipteran insects Journal Article
In: Res. Immunol., vol. 141, no. 9, pp. 910–918, 1990, ISSN: 0923-2494.
BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription
@article{hoffmann_inducible_1990,
title = {The inducible antibacterial peptides of dipteran insects},
author = {Jules A Hoffmann and Danièle Hoffmann},
issn = {0923-2494},
year = {1990},
date = {1990-12-01},
journal = {Res. Immunol.},
volume = {141},
number = {9},
pages = {910--918},
keywords = {Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription},
pubstate = {published},
tppubtype = {article}
}
Schröter H, Mueller C G, Meese K, Nordheim A
Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element Journal Article
In: The EMBO journal, vol. 9, no. 4, pp. 1123–1130, 1990, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors
@article{schroter_synergism_1990,
title = {Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element},
author = {H Schröter and C G Mueller and K Meese and A Nordheim},
issn = {0261-4189},
year = {1990},
date = {1990-04-01},
journal = {The EMBO journal},
volume = {9},
number = {4},
pages = {1123--1130},
abstract = {Transcriptional regulation of the c-fos proto-oncogene requires the serum response element (SRE) which is complexed by a multi-protein assembly observed both in vitro and in vivo. Two protein factors, p67SRF and p62TCF (previously called p62), are required to interact with the SRE for efficient induction of c-fos by serum. By quantitative band shift electrophoresis we measure at least a 50-fold increase in SRE affinity for p67SRF/p62TCF over p67SRF alone. Stoichiometrically we determine that the ternary complex with p62TCF involves p67SRF in dimeric form. We demonstrate that p67SRF is a glycosylated nuclear transcription factor carrying terminal N-acetylglucosamine (GlcNAc) as a post-translational modification. A proteolytic limit digestion product, approximately 13 kd in size, was generated from the p67SRF-SRE complex. This p67SRF-core domain binds SRE, can dimerize with p67SRF and is still able to form a ternary complex with p62TCF. Therefore, three functional activities can be ascribed to this small p67SRF-core domain: specific DNA binding, dimerization and interaction with p62TCF. We demonstrate that these functions map within the p67SRF core fragment containing the region between amino acids 93 and 222.},
keywords = {Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
1989
Reichhart Jean-Marc, Essrich M, Dimarcq Jean-Luc, Hoffmann Danièle, Hoffmann Jules A, Lagueux Marie
Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera). Transcriptional profiles during immunization Journal Article
In: Eur. J. Biochem., vol. 182, no. 2, pp. 423–427, 1989, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Bacterial Proteins, Base Sequence, Blotting, Diptera, DNA, Endoribonucleases, Enterobacter, Enterobacteriaceae, Gene Expression Regulation, Genes, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, messenger, MHC Class II, Northern, reichhart, Ribonuclease H, RNA, Transcription
@article{reichhart_insect_1989,
title = {Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera). Transcriptional profiles during immunization},
author = {Jean-Marc Reichhart and M Essrich and Jean-Luc Dimarcq and Danièle Hoffmann and Jules A Hoffmann and Marie Lagueux},
issn = {0014-2956},
year = {1989},
date = {1989-01-01},
journal = {Eur. J. Biochem.},
volume = {182},
number = {2},
pages = {423--427},
abstract = {We have previously isolated and characterized a family of novel 8-kDa cationic antibacterial peptides synthesized by larvae of Phormia terranovae (Diptera) in response to various injuries. These molecules have been named diptericins. The peptide sequence of diptericin A was used to prepare oligonucleotides for screening cDNA libraries and we report in the present paper the isolation of several cDNA clones encoding diptericin. The analysis of the nucleotide sequences indicates that diptericin is synthesized as a prepeptide which is matured in two steps: (a) cleavage of a signal peptide and (b) amidation of the C-terminal residue. Interestingly, the 3' untranslated region of the mRNA contains a consensus sequence TTATTTAT which is also observed in the mRNA of another insect antibacterial peptide (attacin-related sarcotoxin IIA) and in mRNAs encoding proteins related to the inflammatory response in mammals. Our data illustrate that diptericins form a polymorphic family of immune peptides. The transcription of the diptericin genes is rapidly induced in the fat body after inoculation of bacteria, as evidenced by the transcriptional profile.},
keywords = {Animals, Anti-Bacterial Agents, Bacterial Proteins, Base Sequence, Blotting, Diptera, DNA, Endoribonucleases, Enterobacter, Enterobacteriaceae, Gene Expression Regulation, Genes, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, messenger, MHC Class II, Northern, reichhart, Ribonuclease H, RNA, Transcription},
pubstate = {published},
tppubtype = {article}
}