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Nucleic Acids Research Advance Access published online on November 13, 2007

Nucleic Acids Research, doi:10.1093/nar/gkm985
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© 2007 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.


Molecular Biology

The C-terminal domain of Escherichia coli Hfq is required for regulation

Branislav Vecerek, Lukas Rajkowitsch, Elisabeth Sonnleitner, Renée Schroeder and Udo Bläsi*

Max F. Perutz Laboratories, University of Vienna, Dr. Bohrgasse 9, 1030 Vienna, Austria

*To whom correspondence should be addressed. Tel: ++43-1-4277-54609; Fax: ++43-1-4277-9546; Email: Udo.Blaesi{at}univie.ac.at

Received August 8, 2007. Revised October 18, 2007. Accepted October 21, 2007.

The Escherichia coli RNA chaperone Hfq is involved in riboregulation of target mRNAs by small trans-encoded non-coding (ncRNAs). Previous structural and genetic studies revealed a RNA-binding surface on either site of the Hfq-hexamer, which suggested that one hexamer can bring together two RNAs in a pairwise fashion. The Hfq proteins of different bacteria consist of an evolutionarily conserved core, whereas there is considerable variation at the C-terminus, with the {gamma}- and ß-proteobacteria possessing the longest C-terminal extension. Using different model systems, we show that a C-terminally truncated variant of Hfq (Hfq65), comprising the conserved hexameric core of Hfq, is defective in auto- and riboregulation. Although Hfq65 retained the capacity to bind ncRNAs, and, as evidenced by fluorescence resonance energy transfer assays, to induce structural changes in the ncRNA DsrA, the truncated variant was unable to accommodate two non-complementary RNA oligonucleotides, and was defective in mRNA binding. These studies indicate that the C-terminal extension of E. coli Hfq constitutes a hitherto unrecognized RNA interaction surface with specificity for mRNAs.


The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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