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PMID: 15680978 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Recognition and selection of tRNA in translation.

FEBS letters ·Vol. 579 ·No. 4 ·2005-02-07 ·Pages 938-42

Rodnina MV, Gromadski KB, Kothe U, Wieden HJ

Abstract

Aminoacyl-tRNA (aa-tRNA) is delivered to the ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. The stepwise movement of aa-tRNA from EF-Tu into the ribosomal A site entails a number of intermediates. The ribosome recognizes aa-tRNA through shape discrimination of the codon-anticodon duplex and regulates the rates of GTP hydrolysis by EF-Tu and aa-tRNA accommodation in the A site by an induced fit mechanism. Recent results of kinetic measurements, ribosome crystallography, single molecule FRET measurements, and cryo-electron microscopy suggest the mechanism of tRNA recognition and selection.

MeSH Terms
Crystallography Protein Biosynthesis/physiology RNA, Messenger/genetics,metabolism RNA, Transfer, Amino Acyl/metabolism Ribosomes/chemistry,physiology
Chemicals
RNA, Messenger RNA, Transfer, Amino Acyl
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Rodnina Marina V
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany. [email protected]
Gromadski Kirill B
Kothe Ute
Wieden Hans-Joachim
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2005-02-07
Pages
938-42
Language
English
Region
England
NLM ID
0155157
Subset
IM
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