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Science. 2012 Mar 16;335(6074):1370-2. doi: 10.1126/science.1217443.

Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome.

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  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.

Abstract

In bacteria, the hybrid transfer-messenger RNA (tmRNA) rescues ribosomes stalled on defective messenger RNAs (mRNAs). However, certain gram-negative bacteria have evolved proteins that are capable of rescuing stalled ribosomes in a tmRNA-independent manner. Here, we report a 3.2 angstrom-resolution crystal structure of the rescue factor YaeJ bound to the Thermus thermophilus 70S ribosome in complex with the initiator tRNA(i)(fMet) and a short mRNA. The structure reveals that the C-terminal tail of YaeJ functions as a sensor to discriminate between stalled and actively translating ribosomes by binding in the mRNA entry channel downstream of the A site between the head and shoulder of the 30S subunit. This allows the N-terminal globular domain to sample different conformations, so that its conserved GGQ motif is optimally positioned to catalyze the hydrolysis of peptidyl-tRNA. This structure gives insights into the mechanism of YaeJ function and provides a basis for understanding how it rescues stalled ribosomes.

PMID:
22422986
[PubMed - indexed for MEDLINE]
PMCID:
PMC3377438
Free PMC Article
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