Article abstract
Nature Structural & Molecular Biology 14, 807 - 813 (2007)
Published online: 19 August 2007 | doi:10.1038/nsmb1285
Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA
Mario Schubert1, Karine Lapouge2, Olivier Duss1, Florian C Oberstrass1, Ilian Jelesarov3, Dieter Haas2 & Frédéric H-T Allain1
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.
- Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
- Département de Microbiologie Fondamentale, Université de Lausanne, CH-1015 Lausanne, Switzerland.
- Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Correspondence to: Dieter Haas2 e-mail: dieter.haas@unil.ch
Correspondence to: Frédéric H-T Allain1 e-mail: allain@mol.biol.ethz.ch
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