Publications
2007
Marzi S, Myasnikov A G, Serganov A, Ehresmann C, Romby P, Yusupov M, Klaholz B P
Structured mRNAs regulate translation initiation by binding to the platform of the ribosome Article de journal
Dans: Cell, vol. 130, no. 6, p. 1019-31, 2007, ISBN: 17889647, (0092-8674 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: 5' Untranslated Regions Amino Acid Sequence Base Sequence Binding Sites Cryoelectron Microscopy Escherichia coli/*genetics/metabolism Escherichia coli Proteins/chemistry/genetics/*metabolism *Gene Expression Regulation, Amino Acid Sequence Homology, Bacterial Models, Bacterial/chemistry/*metabolism RNA, Messenger/*metabolism RNA, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation *Peptide Chain Initiation, Nucleic Acid Structural Homology, Protein Time Factors, Ribonucleic Acid Ribosomal Proteins/chemistry/genetics/*metabolism Ribosomes/chemistry/*metabolism/ultrastructure Sequence Homology, ROMBY, Transfer/metabolism Regulatory Sequences, Translational Protein Binding Protein Conformation RNA, Unité ARN
@article{,
title = {Structured mRNAs regulate translation initiation by binding to the platform of the ribosome},
author = {S Marzi and A G Myasnikov and A Serganov and C Ehresmann and P Romby and M Yusupov and B P Klaholz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17889647},
isbn = {17889647},
year = {2007},
date = {2007-01-01},
journal = {Cell},
volume = {130},
number = {6},
pages = {1019-31},
abstract = {Gene expression can be regulated at the level of initiation of protein biosynthesis via structural elements present at the 5' untranslated region of mRNAs. These folded mRNA segments may bind to the ribosome, thus blocking translation until the mRNA unfolds. Here, we report a series of cryo-electron microscopy snapshots of ribosomal complexes directly visualizing either the mRNA structure blocked by repressor protein S15 or the unfolded, active mRNA. In the stalled state, the folded mRNA prevents the start codon from reaching the peptidyl-tRNA (P) site inside the ribosome. Upon repressor release, the mRNA unfolds and moves into the mRNA channel allowing translation initiation. A comparative structure and sequence analysis suggests the existence of a universal stand-by site on the ribosome (the 30S platform) dedicated for binding regulatory 5' mRNA elements. Different types of mRNA structures may be accommodated during translation preinitiation and regulate gene expression by transiently stalling the ribosome.},
note = {0092-8674 (Print)
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {5' Untranslated Regions Amino Acid Sequence Base Sequence Binding Sites Cryoelectron Microscopy Escherichia coli/*genetics/metabolism Escherichia coli Proteins/chemistry/genetics/*metabolism *Gene Expression Regulation, Amino Acid Sequence Homology, Bacterial Models, Bacterial/chemistry/*metabolism RNA, Messenger/*metabolism RNA, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation *Peptide Chain Initiation, Nucleic Acid Structural Homology, Protein Time Factors, Ribonucleic Acid Ribosomal Proteins/chemistry/genetics/*metabolism Ribosomes/chemistry/*metabolism/ultrastructure Sequence Homology, ROMBY, Transfer/metabolism Regulatory Sequences, Translational Protein Binding Protein Conformation RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2004
Mathy N, Pellegrini O, Serganov A, Patel D J, Ehresmann C, Portier C
Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation Article de journal
Dans: Mol Microbiol, vol. 52, no. 3, p. 661-675, 2004, ISBN: 15101974, (0950-382x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/chemistry/genetics/*metabolism Recombinant Fusion Proteins/metabolism Ribosomal Proteins/chemistry/*genetics/*metabolism Sequence Alignment Support, Bacterial Models, EHRESMANN Amino Acid Sequence Base Sequence Escherichia coli Proteins/chemistry/genetics/*metabolism Gene Expression Regulation, Messenger/metabolism RNA, Molecular *Molecular Mimicry Molecular Sequence Data Mutagenesis, Non-U.S. Gov't Support, P.H.S., Ribosomal, Secondary RNA, Site-Directed Nucleic Acid Conformation Protein Structure, U.S. Gov't, Unité ARN
@article{,
title = {Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation},
author = {N Mathy and O Pellegrini and A Serganov and D J Patel and C Ehresmann and C Portier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15101974},
isbn = {15101974},
year = {2004},
date = {2004-01-01},
journal = {Mol Microbiol},
volume = {52},
number = {3},
pages = {661-675},
abstract = {The ribosomal protein S15 binds to 16S rRNA, during ribosome assembly, and to its own mRNA (rpsO mRNA), affecting autocontrol of its expression. In both cases, the RNA binding site is bipartite with a common subsite consisting of a G*U/G-C motif. The second subsite is located in a three-way junction in 16S rRNA and in the distal part of a stem forming a pseudoknot in Escherichia coli rpsO mRNA. To determine the extent of mimicry between these two RNA targets, we determined which amino acids interact with rpsO mRNA. A plasmid carrying rpsO (the S15 gene) was mutagenized and introduced into a strain lacking S15 and harbouring an rpsO-lacZ translational fusion. Analysis of deregulated mutants shows that each subsite of rpsO mRNA is recognized by a set of amino acids known to interact with 16S rRNA. In addition to the G*U/G-C motif, which is recognized by the same amino acids in both targets, the other subsite interacts with amino acids also involved in contacts with helix H22 of 16S rRNA, in the region adjacent to the three-way junction. However, specific S15-rpsO mRNA interactions can also be found, probably with A(-46) in loop L1 of the pseudoknot, demonstrating that mimicry between the two targets is limited.},
note = {0950-382x
Journal Article},
keywords = {16S/chemistry/genetics/*metabolism Recombinant Fusion Proteins/metabolism Ribosomal Proteins/chemistry/*genetics/*metabolism Sequence Alignment Support, Bacterial Models, EHRESMANN Amino Acid Sequence Base Sequence Escherichia coli Proteins/chemistry/genetics/*metabolism Gene Expression Regulation, Messenger/metabolism RNA, Molecular *Molecular Mimicry Molecular Sequence Data Mutagenesis, Non-U.S. Gov't Support, P.H.S., Ribosomal, Secondary RNA, Site-Directed Nucleic Acid Conformation Protein Structure, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2003
Roy H, Becker H D, Reinbolt J, Kern D
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 100, no. 17, p. 9837-9842, 2003, ISBN: 12874385, (0027-8424 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Substrate Specificity Support, Amino Acid Sequence Amino Acids/*metabolism Amino Acyl-tRNA Ligases/chemistry/genetics/*metabolism Catalytic Domain/genetics Cloning, Archaeal Genes, Bacterial Models, Molecular Escherichia coli/genetics/metabolism Genes, Molecular Molecular Sequence Data Phylogeny Protein Conformation Pyrococcus/enzymology/genetics Sequence Homology, Non-U.S. Gov't, Unité ARN
@article{,
title = {When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism},
author = {H Roy and H D Becker and J Reinbolt and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12874385},
isbn = {12874385},
year = {2003},
date = {2003-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {100},
number = {17},
pages = {9837-9842},
abstract = {Faithful protein synthesis relies on a family of essential enzymes called aminoacyl-tRNA synthetases, assembled in a piecewise fashion. Analysis of the completed archaeal genomes reveals that all archaea that possess asparaginyl-tRNA synthetase (AsnRS) also display a second ORF encoding an AsnRS truncated from its anticodon binding-domain (AsnRS2). We show herein that Pyrococcus abyssi AsnRS2, in contrast to AsnRS, does not sustain asparaginyl-tRNAAsn synthesis but is instead capable of converting aspartic acid into asparagine. Functional analysis and complementation of an Escherichia coli asparagine auxotrophic strain show that AsnRS2 constitutes the archaeal homologue of the bacterial ammonia-dependent asparagine synthetase A (AS-A), therefore named archaeal asparagine synthetase A (AS-AR). Primary sequence- and 3D-based phylogeny shows that an archaeal AspRS ancestor originated AS-AR, which was subsequently transferred into bacteria by lateral gene transfer in which it underwent structural changes producing AS-A. This study provides evidence that a contemporary aminoacyl-tRNA synthetase can be recruited to sustain amino acid metabolism.},
note = {0027-8424
Journal Article},
keywords = {Amino Acid Substrate Specificity Support, Amino Acid Sequence Amino Acids/*metabolism Amino Acyl-tRNA Ligases/chemistry/genetics/*metabolism Catalytic Domain/genetics Cloning, Archaeal Genes, Bacterial Models, Molecular Escherichia coli/genetics/metabolism Genes, Molecular Molecular Sequence Data Phylogeny Protein Conformation Pyrococcus/enzymology/genetics Sequence Homology, Non-U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Romby P, Springer M
Bacterial translational control at atomic resolution Article de journal
Dans: Trends Genet, vol. 19, no. 3, p. 155-161, 2003, ISBN: 12615010, (0168-9525 Journal Article Review Review, Tutorial).
Résumé | Liens | BibTeX | Étiquettes: Bacterial *Gene Expression Regulation, Bacterial Models, Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics *Gene Expression Regulation, Biological Models, Enzymologic Genes, Genetic, Messenger/genetics/*metabolism RNA, Molecular Molecular Mimicry Nucleic Acid Conformation Operator Regions (Genetics) RNA, Non-U.S. Gov't Threonine-tRNA Ligase/chemistry/*genetics/metabolism *Translation, ROMBY, Thr/*metabolism RNA-Binding Proteins/metabolism Support, Transfer, Unité ARN
@article{,
title = {Bacterial translational control at atomic resolution},
author = {P Romby and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12615010},
isbn = {12615010},
year = {2003},
date = {2003-01-01},
journal = {Trends Genet},
volume = {19},
number = {3},
pages = {155-161},
abstract = {Translational regulation allows rapid adaptation of protein synthesis to environmental conditions. In prokaryotes, the synthesis of many RNA-binding proteins is regulated by a translational feedback mechanism involving a competition between their natural substrate and their binding site on mRNA, which are often thought to resemble each other. This article describes the case of threonyl-tRNA synthetase, which represses the translation of its own mRNA. Recent data provide the first opportunity to describe at the atomic level both the extent and the limit of mimicry between the way this enzyme recognizes tRNA(Thr) and its regulatory site in mRNA. The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation.},
note = {0168-9525
Journal Article
Review
Review, Tutorial},
keywords = {Bacterial *Gene Expression Regulation, Bacterial Models, Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics *Gene Expression Regulation, Biological Models, Enzymologic Genes, Genetic, Messenger/genetics/*metabolism RNA, Molecular Molecular Mimicry Nucleic Acid Conformation Operator Regions (Genetics) RNA, Non-U.S. Gov't Threonine-tRNA Ligase/chemistry/*genetics/metabolism *Translation, ROMBY, Thr/*metabolism RNA-Binding Proteins/metabolism Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2002
Wagner E G, Altuvia S, Romby P
Antisense RNAs in bacteria and their genetic elements. Chapitre d'ouvrage
Dans: Dunlap, J C; Wu, C. -ting (Ed.): Advances in Genetics: Homology Effects., vol. 46, p. 361-398, Academic Press, 2002, ISBN: 11931231, (0065-2660 Review Review, Academic).
Résumé | Liens | BibTeX | Étiquettes: Antisense/*genetics/metabolism RNA, Bacteria/*genetics/metabolism Bacteriophages/genetics Chromosomes, Bacterial Models, Bacterial/*genetics/metabolism Support, Bacterial/genetics Conjugation, Genetic DNA Replication/genetics DNA Transposable Elements/genetics Gene Expression Regulation, Genetic Mutation Plasmids/genetics RNA, Non-U.S. Gov't, ROMBY, Unité ARN
@inbook{,
title = {Antisense RNAs in bacteria and their genetic elements.},
author = {E G Wagner and S Altuvia and P Romby},
editor = {J C Dunlap and C.-ting Wu},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11931231},
isbn = {11931231},
year = {2002},
date = {2002-01-01},
booktitle = {Advances in Genetics: Homology Effects.},
volume = {46},
pages = {361-398},
publisher = {Academic Press},
abstract = {Antisense RNA-mediated regulation is widespread in bacteria. Most antisense RNA control systems have been found in plasmids, phages, and transposons. Fewer examples were identified in bacterial chromosomes. This chapter summarizes our current knowledge about antisense RNAs with respect to their occurrence, their biological roles, and their diverse mechanisms of action. Examples of cis- or trans-encoded antisense RNAs are discussed, and their properties compared. Most antisense RNAs are posttranscriptionally acting inhibitors of target genes, but a few examples of activator antisense RNAs are known. The implications of RNA structure on topologically and kinetically favored binding pathways are addressed, and solutions that have evolved to permit productive interactions between intricately folded RNAs are discussed. Finally, we describe how particular properties of individual antisense/target RNA systems match their respective biological roles.},
note = {0065-2660
Review
Review, Academic},
keywords = {Antisense/*genetics/metabolism RNA, Bacteria/*genetics/metabolism Bacteriophages/genetics Chromosomes, Bacterial Models, Bacterial/*genetics/metabolism Support, Bacterial/genetics Conjugation, Genetic DNA Replication/genetics DNA Transposable Elements/genetics Gene Expression Regulation, Genetic Mutation Plasmids/genetics RNA, Non-U.S. Gov't, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
2000
Kolb F A, Engdahl H M, Slagter-Jager J G, Ehresmann B, Ehresmann C, Westhof E, Wagner E G, Romby P
Progression of a loop-loop complex to a four-way junction is crucial for the activity of a regulatory antisense RNA Article de journal
Dans: EMBO J, vol. 19, no. 21, p. 5905-5915, 2000, ISBN: 11060041, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Antisense/*chemistry/*genetics/metabolism RNA, Bacterial Models, Bacterial Proteins/genetics Base Sequence Binding, Bacterial/chemistry/genetics/metabolism Support, Competitive DNA Primers/genetics Escherichia coli/chemistry/genetics/metabolism Genes, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation RNA, Non-U.S. Gov't, ROMBY, Unité ARN
@article{,
title = {Progression of a loop-loop complex to a four-way junction is crucial for the activity of a regulatory antisense RNA},
author = {F A Kolb and H M Engdahl and J G Slagter-Jager and B Ehresmann and C Ehresmann and E Westhof and E G Wagner and P Romby},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11060041},
isbn = {11060041},
year = {2000},
date = {2000-01-01},
journal = {EMBO J},
volume = {19},
number = {21},
pages = {5905-5915},
abstract = {The antisense RNA, CopA, regulates the replication frequency of plasmid R1 through inhibition of RepA translation by rapid and specific binding to its target RNA (CopT). The stable CopA-CopT complex is characterized by a four-way junction structure and a side-by-side alignment of two long intramolecular helices. The significance of this structure for binding in vitro and control in vivo was tested by mutations in both CopA and CopT. High rates of stable complex formation in vitro and efficient inhibition in vivo required initial loop-loop complexes to be rapidly converted to extended interactions. These interactions involve asymmetric helix progression and melting of the upper stems of both RNAs to promote the formation of two intermolecular helices. Data presented here delineate the boundaries of these helices and emphasize the need for unimpeded helix propagation. This process is directional, i.e. one of the two intermolecular helices (B) must form first to allow formation of the other (B'). A binding pathway, characterized by a hierarchy of intermediates leading to an irreversible and inhibitory RNA-RNA complex, is proposed.},
note = {0261-4189
Journal Article},
keywords = {Antisense/*chemistry/*genetics/metabolism RNA, Bacterial Models, Bacterial Proteins/genetics Base Sequence Binding, Bacterial/chemistry/genetics/metabolism Support, Competitive DNA Primers/genetics Escherichia coli/chemistry/genetics/metabolism Genes, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation RNA, Non-U.S. Gov't, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Benito Y, Kolb F A, Romby P, Lina G, Etienne J, Vandenesch F
Probing the structure of RNAIII, the Staphylococcus aureus agr regulatory RNA, and identification of the RNA domain involved in repression of protein A expression Article de journal
Dans: RNA, vol. 6, no. 5, p. 668-679, 2000, ISBN: 10836788, (1355-8382 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Antisense/*chemistry/genetics/metabolism RNA, Bacterial Models, Bacterial/*chemistry/genetics/metabolism Ribosomes/metabolism Staphylococcal Protein A/*genetics Staphylococcus aureus/*chemistry/*genetics/metabolism Support, Base Sequence Binding Sites/genetics DNA Primers/genetics Escherichia coli/metabolism Gene Expression Genes, Molecular Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't, ROMBY, Unité ARN
@article{,
title = {Probing the structure of RNAIII, the Staphylococcus aureus agr regulatory RNA, and identification of the RNA domain involved in repression of protein A expression},
author = {Y Benito and F A Kolb and P Romby and G Lina and J Etienne and F Vandenesch},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10836788},
isbn = {10836788},
year = {2000},
date = {2000-01-01},
journal = {RNA},
volume = {6},
number = {5},
pages = {668-679},
abstract = {RNAIII, a 514-nt RNA molecule, regulates the expression of many Staphylococcus aureus genes encoding exoproteins and cell-wall-associated proteins. We have studied the structure of RNAIII in solution, using a combination of chemical and enzymatic probes. A model of the secondary structure was derived from experimental data with the help of computer simulation of RNA folding. The model contains 14 hairpin structures connected by unpaired nucleotides. The data also point to three helices formed by distant nucleotides that close off structural domains. This model was generally compatible with the results of in vivo probing experiments with dimethylsulfate in late exponential-phase cultures. Toe-printing experiments revealed that the ribosome binding site of hld, which is encoded by RNAIII, was accessible to the Escherichia coli 30S ribosomal subunit, suggesting that the in vitro structure represented a translatable form of RNAIII. We also found that, within the 3' end of RNAIII, the conserved hairpin 13 and the terminator form an intrinsic structural domain that exerts specific regulatory activity on protein A gene expression.},
note = {1355-8382
Journal Article},
keywords = {Antisense/*chemistry/genetics/metabolism RNA, Bacterial Models, Bacterial/*chemistry/genetics/metabolism Ribosomes/metabolism Staphylococcal Protein A/*genetics Staphylococcus aureus/*chemistry/*genetics/metabolism Support, Base Sequence Binding Sites/genetics DNA Primers/genetics Escherichia coli/metabolism Gene Expression Genes, Molecular Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1994
Blomberg P, Engdahl H M, Malmgren C, Romby P, Wagner E G
Replication control of plasmid R1: disruption of an inhibitory RNA structure that sequesters the repA ribosome-binding site permits tap-independent RepA synthesis Article de journal
Dans: Mol Microbiol, vol. 12, no. 1, p. 49-60, 1994, ISBN: 7520116, (0950-382x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 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
Poterszman A, Plateau P, Moras D, Blanquet S, Mazauric M H, Kreutzer R, Kern D
Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases Article de journal
Dans: FEBS Lett, vol. 325, no. 3, p. 183-186, 1993, ISBN: 8319804, (0014-5793 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acid Sequence Aspartate-tRNA Ligase/chemistry/*genetics/metabolism Base Sequence Cloning, Bacterial Models, Molecular Crystallization Genes, Molecular Molecular Sequence Data Oligodeoxyribonucleotides Sequence Homology, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Unité ARN
@article{,
title = {Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases},
author = {A Poterszman and P Plateau and D Moras and S Blanquet and M H Mazauric and R Kreutzer and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8319804},
isbn = {8319804},
year = {1993},
date = {1993-01-01},
journal = {FEBS Lett},
volume = {325},
number = {3},
pages = {183-186},
abstract = {The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strain VK-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 A resolution (space group P2(1)2(1)2(1)},
note = {0014-5793
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Aspartate-tRNA Ligase/chemistry/*genetics/metabolism Base Sequence Cloning, Bacterial Models, Molecular Crystallization Genes, Molecular Molecular Sequence Data Oligodeoxyribonucleotides Sequence Homology, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Unité ARN},
pubstate = {published},
tppubtype = {article}
}