Lescure A, Allmang C, Yamada K, Carbon P, Krol A
cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2 Article de journal
Dans: Gene, vol. 291, no. 1-2, p. 279-285, 2002, ISBN: 12095701, (0378-1119 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN
@article{,
title = {cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2},
author = {A Lescure and C Allmang and K Yamada and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12095701},
isbn = {12095701},
year = {2002},
date = {2002-01-01},
journal = {Gene},
volume = {291},
number = {1-2},
pages = {279-285},
abstract = {Selenocysteine and selenoprotein synthesis require a complex molecular machinery in mammals. Among the key players is the RNA-protein complex formed by the selenocysteine insertion sequence (SECIS) binding protein (SBP2) and the SECIS element, an RNA hairpin in the 3' untranslated regions of selenoprotein messenger RNAs (mRNAs). We have isolated the DNA complementary to mRNA of the human SBP2, enabling us to establish that it differs from a previously reported human SBP2-like protein. Examination of the expression pattern revealed that the human SBP2 protein is encoded by a 4 kb long mRNA that is over-expressed in testis. Compared to the rat SBP2 sequence, the human SBP2 protein displays two highly conserved domains with 92 and 95% amino acid identity, the latter one containing the RNA binding domain. The inter-domain section carries 55% sequence identity, the remainder of the SBP2 sequences showing about 65% identity, values lower than expected for two mammalian proteins. Interestingly, we could show that the binding of human SBP2 to the SECIS RNA is stimulated by the selenoprotein-specialized elongation translation factor mSelB/eEFsec.},
note = {0378-1119
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Serganov A, Rak A, Garber M, Reinbolt J, Ehresmann B, Ehresmann C, Grunberg-Manago M, Portier C
Ribosomal protein S15 from Thermus thermophilus--cloning, sequencing, overexpression of the gene and RNA-binding properties of the protein Article de journal
Dans: Eur J Biochem, vol. 246, no. 2, p. 291-300, 1997, ISBN: 9208917, (0014-2956 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/metabolism RNA-Binding Proteins/*genetics/metabolism Ribosomal Proteins/*genetics/metabolism Sequence Homology, Amino Acid Support, Amino Acid Sequence Base Sequence Cloning, Bacterial Escherichia coli/genetics Molecular Sequence Data Plasmids RNA, Molecular DNA, Non-U.S. Gov't Thermus thermophilus/*genetics, Ribosomal, Unité ARN
@article{,
title = {Ribosomal protein S15 from Thermus thermophilus--cloning, sequencing, overexpression of the gene and RNA-binding properties of the protein},
author = {A Serganov and A Rak and M Garber and J Reinbolt and B Ehresmann and C Ehresmann and M Grunberg-Manago and C Portier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9208917},
isbn = {9208917},
year = {1997},
date = {1997-01-01},
journal = {Eur J Biochem},
volume = {246},
number = {2},
pages = {291-300},
abstract = {A 6-kb DNA fragment from an extreme thermophile, Thermus thermophilus, carrying the genes for cytochrome oxidase ba3 subunit I (cbaA) and the ribosomal protein S15 (rpsO) was cloned into Escherichia coli. The gene rpsO was sequenced. The deduced amino acid sequence exhibits 59% identity to the corresponding protein from E. coli. Expression of rpsO in E. coli requires the use of a fully repressed inducible promoter because S15 from T. thermophilus is toxic for E. coli cells. When purified without denaturation from either overproducing E. coli strain or from T. thermophilus ribosomes, the S15 protein is stable and binds a cloned T. thermophilus 16S rRNA fragment (nucleotides 559-753), with low identical dissociation constants (2.5 nM), thus demonstrating that the thermophilic protein folds correctly in a mesophilic bacterium. The rRNA fragment bound corresponds in position and structure to the 16S rRNA fragment of E. coli. A similar high affinity was also found for the binding of S15 from T. thermophilus or E. coli to the corresponding E. coli 16S rRNA fragment, whereas a slightly lower affinity was observed in binding experiments between E. coli S15 and T. thermophilus 16S rRNA fragment. These results suggest that S15 from T. thermophilus recognizes similar determinants in both rRNA fragments. Competition experiments support this conclusion.},
note = {0014-2956
Journal Article},
keywords = {16S/metabolism RNA-Binding Proteins/*genetics/metabolism Ribosomal Proteins/*genetics/metabolism Sequence Homology, Amino Acid Support, Amino Acid Sequence Base Sequence Cloning, Bacterial Escherichia coli/genetics Molecular Sequence Data Plasmids RNA, Molecular DNA, Non-U.S. Gov't Thermus thermophilus/*genetics, Ribosomal, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Vysotskaya V, Tischenko S, Garber M, Kern D, Mougel M, Ehresmann C, Ehresmann B
The ribosomal protein S8 from Thermus thermophilus VK1. Sequencing of the gene, overexpression of the protein in Escherichia coli and interaction with rRNA Article de journal
Dans: Eur J Biochem, vol. 223, no. 2, p. 437-445, 1994, ISBN: 7519982, (0014-2956 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 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}
}
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 Article de journal
Dans: EMBO J, vol. 12, no. 2, p. 607-616, 1993, ISBN: 8440250, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: *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}
}