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Aminoacylation of the anticodon stem by a tRNA-synthetase paralog: relic of an ancient code?
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
2004 (English)In: TIBS -Trends in Biochemical Sciences. Regular ed., ISSN 0968-0004, E-ISSN 1362-4326, Vol. 29, no 10, 519-522 p.Article in journal (Refereed) PublishedText
Abstract [en]

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.

Place, publisher, year, edition, pages
London: Elsevier, 2004. Vol. 29, no 10, 519-522 p.
Keyword [en]
coli yadB gene, escherichia coli, queuosine, biosynthesis, hypothesis, tRNA(Asp), sequence, family, origin
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-122152DOI: 10.1016/j.tibs.2004.08.005ISI: 000224580300003PubMedID: 15450604OAI: diva2:941426
Available from: 2016-06-22 Created: 2016-06-15 Last updated: 2016-06-22Bibliographically approved

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Björk, Glenn R
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Department of Molecular Biology (Faculty of Science and Technology)
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