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Human mitochondrial TyrRS disobeys the tyrosine identity rules.

Authors
  • Bonnefond, Luc
  • Frugier, Magali
  • Giegé, Richard
  • Rudinger-Thirion, Joëlle
Type
Published Article
Journal
RNA (New York, N.Y.)
Publication Date
May 01, 2005
Volume
11
Issue
5
Pages
558–562
Identifiers
PMID: 15840810
Source
Medline
License
Unknown

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.

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