Publications
2003
Geslain R, Martin F, Camasses A, Eriani G
A yeast knockout strain to discriminate between active and inactive tRNA molecules Journal Article
In: Nucleic Acids Res, vol. 31, no. 16, pp. 4729-4737, 2003, ISBN: 12907713, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acyl-tRNA Ligases/metabolism Arginine/genetics/metabolism Base Sequence Blotting, Arg/chemistry/*genetics/metabolism Saccharomyces cerevisiae/*genetics Support, ERIANI, Molecular Hydrogen-Ion Concentration Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Northern Cloning, Site-Directed Mutation Nucleic Acid Conformation RNA, Transfer, Unité ARN
@article{,
title = {A yeast knockout strain to discriminate between active and inactive tRNA molecules},
author = {R Geslain and F Martin and A Camasses and G Eriani},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12907713},
isbn = {12907713},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {16},
pages = {4729-4737},
abstract = {Here we report the construction of a yeast genetic screen designed to identify essential residues in tRNA(Arg). The system consists of a tRNA(Arg) knockout strain and a set of vectors designed to rescue and select for variants of tRNA(Arg). By plasmid shuffling we selected inactive tRNA mutants that were further analyzed by northern blotting. The mutational analysis focused on the tRNA D and anticodon loops that contact the aminoacyl-tRNA synthetase. The anticodon triplet was excluded from the analysis because of its role in decoding the Arg codons. Most of the inactivating mutations are residues involved in tertiary interactions. These mutations had dramatic effects on tRNA(Arg) abundance. Other inactivating mutations were located in the anticodon loop, where they did not affect transcription and aminoacylation but probably altered interaction with the translation machinery. No lethal effects were observed when residues 16, 20 and 38 were individually mutated, despite the fact that they are involved in sequence-specific interactions with the aminoacyl-tRNA synthetase. However, the steady-state levels of the aminoacylated forms of U20A and U20G were decreased by a factor of 3.5-fold in vivo. This suggests that, unlike in the Escherichia coli tRNA(Arg):ArgRS system where residue 20 (A) is a major identity element, in yeast this position is of limited consequence.},
note = {1362-4962
Journal Article},
keywords = {Amino Acyl-tRNA Ligases/metabolism Arginine/genetics/metabolism Base Sequence Blotting, Arg/chemistry/*genetics/metabolism Saccharomyces cerevisiae/*genetics Support, ERIANI, Molecular Hydrogen-Ion Concentration Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Northern Cloning, Site-Directed Mutation Nucleic Acid Conformation RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2002
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 Journal Article
In: Gene, vol. 291, no. 1-2, pp. 279-285, 2002, ISBN: 12095701, (0378-1119 Journal Article).
Abstract | Links | BibTeX | Tags: 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}
}