"Aminoacylation of the anticodon stem by a tRNA-synthetase paralog: relic of an ancient code?"

Grosjean H, de Crecy-Lagard V, Bjork GR



Published 2004-10-01 in Trends Biochem Sci volume 29 .

Pubmed ID: 15450604
DOI identifier: -

Abstract:
The activation and charging of amino acids onto the acceptor stems of their cognate tRNAs are the housekeeping functions of aminoacyl-tRNA synthetases. The availability of whole genome sequences has revealed the existence of synthetase-like proteins that have other functions linked to different aspects of cell metabolism and physiology. In eubacteria, a paralog of glutamyl-tRNA synthetase, which lacks the tRNA-binding domain, was found to aminoacylate tRNA(Asp) not on the 3'-hydroxyl group of the acceptor stem but on a cyclopentene diol of the modified nucleoside queuosine present at the wobble position of anticodon loop. This modified nucleoside might be a relic of an ancient code.


Last modification of this entry: Sept. 6, 2012