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-Structure paper
Title | Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 39, Issue 11, Page 4900-4915, Year 2011 |
Publish date | Feb 17, 2011 |
Authors | Mads Beich-Frandsen / Branislav Vecerek / Petr V Konarev / Björn Sjöblom / Karin Kloiber / Hermann Hämmerle / Lukas Rajkowitsch / Andrew J Miles / Georg Kontaxis / B A Wallace / Dimitri I Svergun / Robert Konrat / Udo Bläsi / Kristina Djinovic-Carugo / |
PubMed Abstract | The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily ...The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in length. Although the structure of the conserved core has been elucidated for several Hfq proteins, no structural information has yet been obtained for the C-terminus. Using bioinformatics, nuclear magnetic resonance spectroscopy, synchrotron radiation circular dichroism (SRCD) spectroscopy and small angle X-ray scattering we provide for the first time insights into the conformation and dynamic properties of the C-terminal extension of Hfq(Ec). These studies indicate that the C-termini are flexible and extend laterally away from the hexameric core, displaying in this way features typical of intrinsically disordered proteins that facilitate intermolecular interactions. We identified a minimal, intrinsically disordered region of the C-terminus supporting the interactions with longer RNA fragments. This minimal region together with rest of the C-terminal extension provides a flexible moiety capable of tethering long and structurally diverse RNA molecules. Furthermore, SRCD spectroscopy supported the hypothesis that RNA fragments exceeding a certain length interact with the C-termini of Hfq(Ec). |
External links | Nucleic Acids Res / PubMed:21330354 / PubMed Central |
Methods | SAS (X-ray synchrotron) |
Structure data | SASDAG5: |
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