Publications
2004
Théobald-Dietrich A, Frugier M, Giege R, Rudinger-Thirion J
Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA Article de journal
Dans: Nucleic Acids Res, vol. 32, no. 3, p. 1091-1096, 2004, ISBN: 14872064, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/metabolism Base Sequence Lysine/*analogs & derivatives/*metabolism Lysine-tRNA Ligase/metabolism Methanosarcina barkeri/genetics Mitochondria/genetics Molecular Sequence Data Nucleic Acid Conformation Peptide Elongation Factor Tu/*metabolism RNA, Archaeal/chemistry/*metabolism RNA, FRUGIER, Non-U.S. Gov't Yeasts/enzymology, Ser/chemistry Selenocysteine/metabolism Support, Transfer, Transfer/chemistry/*metabolism RNA, Unité ARN
@article{,
title = {Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA},
author = {A Théobald-Dietrich and M Frugier and R Giege and J Rudinger-Thirion},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14872064},
isbn = {14872064},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {3},
pages = {1091-1096},
abstract = {The newly discovered tRNA(Pyl) is involved in specific incorporation of pyrrolysine in the active site of methylamine methyltransferases in the archaeon Methanosarcina barkeri. In solution probing experiments, a transcript derived from tRNA(Pyl) displays a secondary fold slightly different from the canonical cloverleaf and interestingly similar to that of bovine mitochondrial tRNA(Ser)(uga). Aminoacylation of tRNA(Pyl) transcript by a typical class II synthetase, LysRS from yeast, was possible when its amber anticodon CUA was mutated into a lysine UUU anticodon. Hydrolysis protection assays show that lysylated tRNA(Pyl) can be recognized by bacterial elongation factor. This indicates that no antideterminant sequence is present in the body of the tRNA(Pyl) transcript to prevent it from interacting with EF-Tu, in contrast with the otherwise functionally similar tRNA(Sec) that mediates selenocysteine incorporation.},
note = {1362-4962
Journal Article},
keywords = {Anticodon/metabolism Base Sequence Lysine/*analogs & derivatives/*metabolism Lysine-tRNA Ligase/metabolism Methanosarcina barkeri/genetics Mitochondria/genetics Molecular Sequence Data Nucleic Acid Conformation Peptide Elongation Factor Tu/*metabolism RNA, Archaeal/chemistry/*metabolism RNA, FRUGIER, Non-U.S. Gov't Yeasts/enzymology, Ser/chemistry Selenocysteine/metabolism Support, Transfer, Transfer/chemistry/*metabolism RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}