Publications
1996
Sissler M, Giege R, Florentz C
Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts Article de journal
Dans: EMBO J, vol. 15, no. 18, p. 5069-5076, 1996, ISBN: 8890180, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: *Anticodon Arginine/*metabolism Base Sequence Kinetics Molecular Sequence Data Nucleic Acid Conformation RNA, Arg/*chemistry/metabolism RNA, Asp/chemistry/metabolism Saccharomyces cerevisiae Support, FLORENTZ, Fungal/*chemistry/metabolism RNA, Non-U.S. Gov't, SISSLER, Transfer, Unité ARN
@article{,
title = {Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts},
author = {M Sissler and R Giege and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8890180},
isbn = {8890180},
year = {1996},
date = {1996-01-01},
journal = {EMBO J},
volume = {15},
number = {18},
pages = {5069-5076},
abstract = {Yeast arginyl-tRNA synthetase recognizes the non-modified wild-type transcripts derived from both yeast tRNA(Arg) and tRNA(Asp) with equal efficiency. It discriminates its cognate natural substrate, tRNA(Arg), from non-cognate tRNA(Asp) by a negative discrimination mechanism whereby a single methyl group acts as an anti-determinant. Considering these facts, recognition elements responsible for specific arginylation in yeast have been searched by studying the in vitro arginylation properties of a series of transcripts derived from yeast tRNA(Asp), considered as an arginine isoacceptor tRNA. In parallel, experiments on similar tRNA(Arg) transcripts were performed. Unexpectedly, in the tRNA(Arg) context, arginylation is basically linked to the presence of residue C35, whereas in the tRNA(Asp) context, it is deeply related to that of C36 and G37 but is insensitive to the nucleotide at position 35. Each of these nucleotides present in one host, is absent in the other host tRNA. Thus, arginine identity is dependent on two different specific recognition sets according to the tRNA framework investigated.},
note = {0261-4189
Journal Article},
keywords = {*Anticodon Arginine/*metabolism Base Sequence Kinetics Molecular Sequence Data Nucleic Acid Conformation RNA, Arg/*chemistry/metabolism RNA, Asp/chemistry/metabolism Saccharomyces cerevisiae Support, FLORENTZ, Fungal/*chemistry/metabolism RNA, Non-U.S. Gov't, SISSLER, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Yeast arginyl-tRNA synthetase recognizes the non-modified wild-type transcripts derived from both yeast tRNA(Arg) and tRNA(Asp) with equal efficiency. It discriminates its cognate natural substrate, tRNA(Arg), from non-cognate tRNA(Asp) by a negative discrimination mechanism whereby a single methyl group acts as an anti-determinant. Considering these facts, recognition elements responsible for specific arginylation in yeast have been searched by studying the in vitro arginylation properties of a series of transcripts derived from yeast tRNA(Asp), considered as an arginine isoacceptor tRNA. In parallel, experiments on similar tRNA(Arg) transcripts were performed. Unexpectedly, in the tRNA(Arg) context, arginylation is basically linked to the presence of residue C35, whereas in the tRNA(Asp) context, it is deeply related to that of C36 and G37 but is insensitive to the nucleotide at position 35. Each of these nucleotides present in one host, is absent in the other host tRNA. Thus, arginine identity is dependent on two different specific recognition sets according to the tRNA framework investigated.