Title |
Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB
|
---|---|
Published in |
Frontiers in Microbiology, March 2014
|
DOI | 10.3389/fmicb.2014.00113 |
Pubmed ID | |
Authors |
Emmanuel Giudice, Kevin Macé, Reynald Gillet |
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. |
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Demographic breakdown
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Mendeley readers
Geographical breakdown
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Researcher | 11 | 15% |
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Student > Master | 8 | 11% |
Unspecified | 6 | 8% |
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Unknown | 7 | 10% |
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Immunology and Microbiology | 3 | 4% |
Other | 6 | 8% |
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