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Dealing with stable structures at ribosome binding sites: bacterial translation and ribosome standby.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. (Wagner)
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. (Wagner)
2007 (English)In: RNA Biology, ISSN 1547-6286, Vol. 4, no 3, 113-117 p.Article in journal (Refereed) Published
Abstract [en]

Bacterial ribosomes have great difficulties to initiate translation on stable structures within mRNAs. Translational coupling and induced structure changes are strategies to open up inhibitory RNA structures encompassing ribosome binding sites (RBS). There are, however, mRNAs in which stable structures are not unfolded, but that are nevertheless efficiently initiated at high rates. de Smit and van Duin(1) proposed a "ribosome standby" model to theoretically solve this paradox: the 30S ribosome binds nonspecifically to an accessible site on the mRNA (standby site), waiting for a transient opening of a stable RBS hairpin. Upon unfolding, the 30S subunit relocates to form a productive initiation complex. Recent reports have provided experimental support for this model. This review will describe and compare two different flavors of standby sites, their properties, and their likely implications. We also discuss the possibility that ribosome standby may be a more general strategy to obtain high translation rates.

Place, publisher, year, edition, pages
2007. Vol. 4, no 3, 113-117 p.
Keyword [en]
ribosome, standby site, RNA structure, translational control, antisense RNA, tisAB mRNA, translation initiation.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-87450PubMedID: 18094628OAI: oai:DiVA.org:uu-87450DiVA: diva2:132409
Available from: 2008-12-18 Created: 2008-12-18 Last updated: 2014-05-28Bibliographically approved

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