Format

Send to

Choose Destination
See comment in PubMed Commons below
Nat Struct Mol Biol. 2007 Sep;14(9):807-13. Epub 2007 Aug 19.

Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.

Author information

1
Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.

Abstract

Proteins of the RsmA/CsrA family are global translational regulators in many bacterial species. We have determined the solution structure of a complex formed between the RsmE protein, a member of this family from Pseudomonas fluorescens, and a target RNA encompassing the ribosome-binding site of the hcnA gene. The RsmE homodimer with its two RNA-binding sites makes optimal contact with an 5'-A/UCANGGANGU/A-3' sequence in the mRNA. When tightly gripped by RsmE, the ANGGAN core folds into a loop, favoring the formation of a 3-base-pair stem by flanking nucleotides. We validated these findings by in vivo and in vitro mutational analyses. The structure of the complex explains well how, by sequestering the Shine-Dalgarno sequence, the RsmA/CsrA proteins repress translation.

PMID:
17704818
DOI:
10.1038/nsmb1285
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Support Center