The transorientation hypothesis for codon recognition during protein synthesis

Nature
Anne B Simonson, James A Lake

Abstract

During decoding, a codon of messenger RNA is matched with its cognate aminoacyl-transfer RNA and the amino acid carried by the tRNA is added to the growing protein chain. Here we propose a molecular mechanism for the decoding phase of translation: the transorientation hypothesis. The model incorporates a newly identified tRNA binding site and utilizes a flip between two tRNA anticodon loop structures, the 5'-stacked and the 3'-stacked conformations. The anticodon loop acts as a three-dimensional hinge permitting rotation of the tRNA about a relatively fixed codon-anticodon pair. This rotation, driven by a conformational change in elongation factor Tu involving GTP hydrolysis, transorients the incoming tRNA into the A site from the D site of initial binding and decoding, where it can be proofread and accommodated. The proposed mechanisms are compatible with the known structures, conformations and functions of the ribosome and its component parts including tRNAs and EF-Tu, in both the GTP and GDP states.

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Citations

Apr 23, 2003·Molecular and Biochemical Parasitology·H Y Xue, D R Forsdyke
Nov 30, 2002·Biochimie·Marina V RodninaWolfgang Wintermeyer
Jul 3, 2002·The EMBO Journal·Mikel ValleJoachim Frank
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Jun 28, 2018·Genome Biology and Evolution·James A LakeJanet S Sinsheimer
Aug 1, 2009·EcoSal Plus·Steven T Gregory
Sep 14, 2002·Science·Feng Gong, Charles Yanofsky

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