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Nucleic Acids Research 2006 34(2):709-720; doi:10.1093/nar/gkj464
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Published online 30 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
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Article

Hfq variant with altered RNA binding functions

Katarzyna Ziolkowska, Philippe Derreumaux1, Marc Folichon, Olivier Pellegrini, Philippe Régnier, Irina V. Boni2 and Eliane Hajnsdorf*

‘Régulation de l'Expression Génétique chez les Microorganismes’ UPR CNRS no. 9073 conventionnée avec l'Université Paris 7, Denis Diderot, Paris, France 1‘Laboratoire de Biochimie Théorique’ UPR CNRS no. 9080 conventionnée avec l'Université Paris 7 Denis Diderot, Paris, France 2Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences 117997 Moscow, Russia

*To whom correspondence should be addressed at UPR CNRS 9073, conventionnée avec l'Université Paris 7, Denis Diderot, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France. Tel: +33 1 58 41 51 26; Fax: +33 1 58 41 50 20; Email: Eliane.Hajnsdorf{at}ibpc.fr

Received October 6, 2005. Revised December 19, 2005. Accepted January 7, 2006.

The interaction between Hfq and RNA is central to multiple regulatory processes. Using site-directed mutagenesis, we have found a missense mutation in Hfq (V43R) which strongly affects2 the RNA binding capacity of the Hfq protein and its ability to stimulate poly(A) tail elongation by poly(A)-polymerase in vitro. In vivo, overexpression of this Hfq variant fails to stimulate rpoS–lacZ expression and does not restore a normal growth rate in hfq null mutant. Cells in which the wild-type gene has been replaced by the hfqV43R allele exhibit a phenotype intermediate between those of the wild-type and of the hfq minus or null strains. This missense mutation derepresses Hfq synthesis. However, not all Hfq functions are affected by this mutation. For example, HfqV43R represses OppA synthesis as strongly as the wild-type protein. The dominant negative effect of the V43R mutation over the wild-type allele suggests that hexamers containing variant and genuine subunits are presumably not functional. Finally, molecular dynamics studies indicate that the V43R substitution mainly changes the position of the K56 and Y55 side chains involved in the Hfq–RNA interaction but has probably no effect on the folding and the oligomerization of the protein.


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