RNAi Europe
Print ISSN: 1547-6286; Online ISSN: 1555-8584


Recommend RNA Biology to your librarian for 2008. Download form here.

Sign up for Table of Contents Alerts!

home subscribe search archive forthcoming

Email this page Print this page

Point of View

Dealing with stable structures at ribosome binding sites: Bacterial translation and ribosome standby

Cecilia Unoson and E. Gerhart H. Wagner

volume 4 | issue 3

july-december

This is an open-access article

 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

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 nevertheless are efficiently initiated at high rates. de Smit and van Duin1 proposed a "ribosome standby" model to theoretically solve this paradox: the 30S ribosome binds non-specifically 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.

Authors

Cecilia Unoson

Department of Cell and Molecular Biology; Biomedical Center; Uppsala University; Uppsala, Sweden

E. Gerhart H. Wagner

Department of Cell and Molecular Biology; Biomedical Center; Uppsala University; Uppsala, Sweden


This is an open-access article

 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.