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EMBO Rep. 2008 Jul;9(7):629-35. doi: 10.1038/embor.2008.104. Epub 2008 Jun 13.

Bringing order to translation: the contributions of transfer RNA anticodon-domain modifications.

Author information

  • Department of Molecular and Structural Biochemistry, 128 Polk Hall, Campus Box 7622, North Carolina State University, Raleigh, North Carolina 27695-7622, USA. paul_agris@ncsu.edu

Abstract

The biosynthesis of RNA includes its post-transcriptional modifications, and the crucial functions of these modifications have supported their conservation within all three kingdoms. For example, the modifications located within or adjacent to the anticodon of the transfer RNA (tRNA) enhance the accuracy of codon binding, maintain the translational reading frame and enable translocation of the tRNA from the A-site to the P-site of the ribosome. Although composed of different chemistries, the more than 70 known modifications of tRNA have in common their ability to reduce conformational dynamics, and to bring order to the internal loops and hairpin structures of RNA. The modified nucleosides of the anticodon domain of tRNA restrict its dynamics and shape its architecture; therefore, the need of the ribosome to constrain or remodel each tRNA to fit the decoding site is diminished. This concept reduces an entropic penalty for translation and provides a physicochemical basis for the conservation of RNA modifications in general.

PMID:
18552770
[PubMed - indexed for MEDLINE]
PMCID:
PMC2475317
Free PMC Article
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