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Front Microbiol. 2014 Mar 21;5:113. doi: 10.3389/fmicb.2014.00113. eCollection 2014.

Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB.

Author information

1
Translation and Folding Team, Université de Rennes 1, CNRS UMR 6290 IGDR Rennes, France.
2
Translation and Folding Team, Université de Rennes 1, CNRS UMR 6290 IGDR Rennes, France ; Institut Universitaire de France France.

Abstract

Ribosome stalling is a serious issue for cell survival. In bacteria, the primary rescue system is trans-translation, performed by tmRNA and its protein partner small protein B (SmpB). Since its discovery almost 20 years ago, biochemical, genetic, and structural studies have paved the way to a better understanding of how this sophisticated process takes place at the cellular and molecular levels. Here we describe the molecular details of trans-translation, with special mention of recent cryo-electron microscopy and crystal structures that have helped explain how the huge tmRNA-SmpB complex targets and delivers stalled ribosomes without interfering with canonical translation.

KEYWORDS:

SmpB; ribosome; structure; tmRNA; trans-translation

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