tRNA/mRNA Mimicry by tmRNA and SmpB inTrans-Translation

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tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation

Since accurate translation from mRNA to protein is critical to survival, cells have developed translational quality control systems. Bacterial ribosomes stalled on truncated mRNA are rescued by a system involving tmRNA and SmpB referred to as trans-translation. Here, we review current understanding of the mechanism of trans-translation. Based on results obtained by using directed hydroxyl radic...

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In the recent years, a wealth of genetic, biochemical and structural data focusing on various steps of bacterial trans-translation was reported. The early events, from stalled ribosome recognition, pre-accommodation to translocation have been recently investigated in great details. In comparison, the later events including 'elongation-termination' onto tmRNA reading frame and ribosome recycling...

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Ends of the line for tmRNA-SmpB

Genes for the RNA tmRNA and protein SmpB, partners in the trans-translation process that rescues stalled ribosomes, have previously been found in all bacteria and some organelles. During a major update of The tmRNA Website (relocated to http://bioinformatics.sandia.gov/tmrna), including addition of an SmpB sequence database, we found some bacteria that lack functionally significant regions of S...

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

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...

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Decoding in the absence of a codon by tmRNA and SmpB in the ribosome.

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 resol...

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ژورنال

عنوان ژورنال: Journal of Nucleic Acids

سال: 2011

ISSN: 2090-021X

DOI: 10.4061/2011/130581