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Enzymatic conversion of cytidine to lysidine in anticodon of bacterial isoleucyl-tRNA--an alternative way of RNA editing
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 4, 165-168 p.Article in journal (Refereed) Published
Abstract [en]

In most organisms, the AUA triplet codes for isoleucine (Ile), whereas in a few organelles it codes for methionine (Met). In bacteria, this A-ending triplet is decoded by an unusual tRNA harboring a Met anticodon CAU, where cytidine at the wobble position 34 (C34) is posttranscriptionally modified to a 2-lysyl cytidine (lysidine), abbreviated as (k2C). Now, the bacterial gene tilS, which encodes the enzyme catalyzing the lysylation of C34 in the precursor tRNAIle(CAU), thereby leading to the formation of tRNAIle(k2CAU), has been identified. The formation of lysidine by this essential enzyme allows recognition of tRNAIle(k2CAU) by Ile-tRNA synthetase and switches the base pairing of the tRNA from AUG (Met) to AUA (Ile). This base change is reminiscent of C-to-U type of RNA editing of some mitochondrial tRNAs.

 

Place, publisher, year, edition, pages
Amsterdam: Int. union of biochemistry and Elsevier/North-Holland , 2004. Vol. 29, no 4, 165-168 p.
Keyword [en]
Amino Acyl-tRNA Synthetases/chemistry/*metabolism, Anticodon/genetics/*metabolism, Base Pairing, Cytidine/chemistry/genetics/*metabolism, Escherichia coli Proteins/*metabolism, Isoleucine-tRNA Ligase/metabolism, Lysine/*analogs & derivatives/chemistry/genetics/*metabolism, Methionine-tRNA Ligase/metabolism, Models; Chemical, Molecular Structure, Pyrimidine Nucleosides/chemistry/genetics/*metabolism, RNA Editing, RNA; Transfer; Ile/genetics/*metabolism
Identifiers
URN: urn:nbn:se:umu:diva-16733DOI: 10.1016/j.tibs.2004.02.009PubMedID: 15124629OAI: oai:DiVA.org:umu-16733DiVA: diva2:156406
Available from: 2007-10-09 Created: 2007-10-09 Last updated: 2017-12-14Bibliographically approved

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