Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs.

Abstract:

:Ribosomes translate genetic information encoded by mRNAs into protein chains with high fidelity. Truncated mRNAs lacking a stop codon will cause the synthesis of incomplete peptide chains and stall translating ribosomes. In bacteria, a ribonucleoprotein complex composed of tmRNA, a molecule that combines the functions of tRNAs and mRNAs, and small protein B (SmpB) rescues stalled ribosomes. The SmpB-tmRNA complex binds to the stalled ribosome, allowing translation to resume at a short internal tmRNA open reading frame that encodes a protein degradation tag. The aberrant protein is released when the ribosome reaches the stop codon at the end of the tmRNA open reading frame and the fused peptide tag targets it for degradation by cellular proteases. The recently determined NMR structures of SmpB, the crystal structure of the SmpB-tmRNA complex and the cryo-EM structure of the SmpB-tmRNA-EF-Tu-ribosome complex have provided first detailed insights into the intricate mechanisms involved in ribosome rescue.

journal_name

Curr Opin Struct Biol

authors

Haebel PW,Gutmann S,Ban N

doi

10.1016/j.sbi.2004.01.010

subject

Has Abstract

pub_date

2004-02-01 00:00:00

pages

58-65

issue

1

eissn

0959-440X

issn

1879-033X

pii

S0959440X04000119

journal_volume

14

pub_type

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