Journal
SCIENCE
Volume 335, Issue 6074, Pages 1366-1369Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1217039
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Funding
- MRC [U105184332]
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Boehringer Ingelheim Fonds
- [ANR-08JCJC-0027-01]
- [ANR-09-MIE]
- MRC [MC_U105184332] Funding Source: UKRI
- Medical Research Council [MC_U105184332] Funding Source: researchfish
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In bacteria, ribosomes stalled at the end of truncated messages are rescued by transfer-messenger RNA (tmRNA), a bifunctional molecule that acts as both a transfer RNA (tRNA) and a messenger RNA (mRNA), and SmpB, a small protein that works in concert with tmRNA. Here, we present the crystal structure of a tmRNA fragment, SmpB and elongation factor Tu bound to the ribosome at 3.2 angstroms resolution. The structure shows how SmpB plays the role of both the anticodon loop of tRNA and portions of mRNA to facilitate decoding in the absence of an mRNA codon in the A site of the ribosome and explains why the tmRNA-SmpB system does not interfere with normal translation.
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