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Nucleic Acids Research Advance Access originally published online on November 27, 2006
Nucleic Acids Research 2006 34(22):6549-6560; doi:10.1093/nar/gkl911
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Nucleic Acids Research, 2006, Vol. 34, No. 22 6549-6560
© 2006 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence

Sylvain Durand, Graziella Richard, Marco Bisaglia1, Soumaya Laalami, François Bontems1 and Marc Uzan*

Institut Jacques Monod. UMR7592 CNRS-Universités Paris 6 and Paris 7. 2 Place Jussieu, 75251 Paris Cedex 05, France 1 ICSN-RMN, Institut de Chimie des Substances Naturelles, CNRS, 91190 Gif sur Yvette and Ecole Polytechnique 91128 Palaiseau, France

*To whom correspondence should be addressed. Tel: 33-1 44277973; Fax: 33-1 44275716; Email: uzan{at}ijm.jussieu.fr

Received September 22, 2006. Revised October 13, 2006. Accepted October 13, 2006.

The T4 RegB endoribonuclease cleaves specifically in the middle of the -GGAG- sequence, leading to inactivation and degradation of early phage mRNAs. In vitro, RegB activity is very weak but can be enhanced 10- to 100-fold by the Escherichia coli ribosomal protein S1. Not all RNAs carrying the GGAG motif are cleaved by RegB, suggesting that additional information is required to obtain a complete RegB target site. In this work, we find that in the presence of S1, the RegB target site is an 11 nt long single-stranded RNA carrying the 100% conserved GGA triplet at the 5' end and a degenerate, A-rich, consensus sequence immediately downstream. Our data support the notion that RegB alone recognizes only the trinucleotide GGA, which it cleaves very inefficiently, and that stimulation of RegB activity by S1 depends on the nucleotide immediately 3' to -GGA-.

Present address: Marco Bisaglia, Institute for Biomolecular Chemistry, CNR, Department of Chemical Sciences, University of Padova, Via F. Marzolo 1, 35131, Padova, Italy


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P. Aliprandi, C. Sizun, J. Perez, F. Mareuil, S. Caputo, J.-L. Leroy, B. Odaert, S. Laalami, M. Uzan, and F. Bontems
S1 Ribosomal Protein Functions in Translation Initiation and Ribonuclease RegB Activation Are Mediated by Similar RNA-Protein Interactions: AN NMR AND SAXS ANALYSIS
J. Biol. Chem., May 9, 2008; 283(19): 13289 - 13301.
[Abstract] [Full Text] [PDF]


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