Publications
2005
Bonnefond L, Frugier M, Giege R, Rudinger-Thirion J
Human mitochondrial TyrRS disobeys the tyrosine identity rules Article de journal
Dans: RNA, vol. 11, no. 5, p. 558-562, 2005, ISBN: 15840810, (1355-8382 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Base Sequence Catalytic Domain Humans Mitochondria/*enzymology Molecular Sequence Data RNA, FRUGIER, Non-U.S. Gov't Substrate Specificity Tyrosine/genetics/*metabolism Tyrosine-tRNA Ligase/chemistry/*metabolism, Transfer, Tyr/genetics/*metabolism Research Support, Unité ARN
@article{,
title = {Human mitochondrial TyrRS disobeys the tyrosine identity rules},
author = {L Bonnefond 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=15840810},
isbn = {15840810},
year = {2005},
date = {2005-01-01},
journal = {RNA},
volume = {11},
number = {5},
pages = {558-562},
abstract = {Human tyrosyl-tRNA synthetase from mitochondria (mt-TyrRS) presents dual sequence features characteristic of eubacterial and archaeal TyrRSs, especially in the region containing amino acids recognizing the N1-N72 tyrosine identity pair. This would imply that human mt-TyrRS has lost the capacity to discriminate between the G1-C72 pair typical of eubacterial and mitochondrial tRNATyr and the reverse pair C1-G72 present in archaeal and eukaryal tRNATyr. This expectation was verified by a functional analysis of wild-type or mutated tRNATyr molecules, showing that mt-TyrRS aminoacylates with similar catalytic efficiency its cognate tRNATyr with G1-C72 and its mutated version with C1-G72. This provides the first example of a TyrRS lacking specificity toward N1-N72 and thus of a TyrRS disobeying the identity rules. Sequence comparisons of mt-TyrRSs across phylogeny suggest that the functional behavior of the human mt-TyrRS is conserved among all vertebrate mt-TyrRSs.},
note = {1355-8382
Journal Article},
keywords = {Amino Acid Sequence Base Sequence Catalytic Domain Humans Mitochondria/*enzymology Molecular Sequence Data RNA, FRUGIER, Non-U.S. Gov't Substrate Specificity Tyrosine/genetics/*metabolism Tyrosine-tRNA Ligase/chemistry/*metabolism, Transfer, Tyr/genetics/*metabolism Research Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Human tyrosyl-tRNA synthetase from mitochondria (mt-TyrRS) presents dual sequence features characteristic of eubacterial and archaeal TyrRSs, especially in the region containing amino acids recognizing the N1-N72 tyrosine identity pair. This would imply that human mt-TyrRS has lost the capacity to discriminate between the G1-C72 pair typical of eubacterial and mitochondrial tRNATyr and the reverse pair C1-G72 present in archaeal and eukaryal tRNATyr. This expectation was verified by a functional analysis of wild-type or mutated tRNATyr molecules, showing that mt-TyrRS aminoacylates with similar catalytic efficiency its cognate tRNATyr with G1-C72 and its mutated version with C1-G72. This provides the first example of a TyrRS lacking specificity toward N1-N72 and thus of a TyrRS disobeying the identity rules. Sequence comparisons of mt-TyrRSs across phylogeny suggest that the functional behavior of the human mt-TyrRS is conserved among all vertebrate mt-TyrRSs.