| Literature DB >> 20019758 |
Sharief Barends1, Martin Zehl, Sylwia Bialek, Ellen de Waal, Bjørn A Traag, Joost Willemse, Ole Nørregaard Jensen, Erik Vijgenboom, Gilles P van Wezel.
Abstract
The transfer-messenger RNA (tmRNA)-mediated trans-translation mechanism is highly conserved in bacteria and functions primarily as a system for the rescue of stalled ribosomes and the removal of aberrantly produced proteins. Here, we show that in the antibiotic-producing soil bacterium Streptomyces coelicolor, trans-translation has a specialized role in stress management. Analysis of proteins that were carboxy-terminally His(8)-tagged by a recombinant tmRNA identified only 10 targets, including the stress proteins: DnaK heat-shock protein 70, thiostrepton-induced protein A, universal stress protein A, elongation factor Tu3, and the cell-cycle control proteins DasR, SsgA, SsgF and SsgR. Although tmRNA-tagged proteins are degraded swiftly, the translation of dnaK and dasR messenger RNAs (mRNAs) depends fully on tmRNA, whereas transcription is unaffected. The data unveil a surprisingly dedicated functionality for tmRNA, promoting the translation of the same mRNA it targets, at the expense of sacrificing the first nascent protein. In streptomycetes, tmRNA has evolved into a dedicated task force that ensures the instantaneous response to the exposure to stress.Entities:
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Year: 2009 PMID: 20019758 PMCID: PMC2828758 DOI: 10.1038/embor.2009.255
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807