Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.

Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.
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DOI:
10.1093/nar/gkq1346
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发表时间:
2011-06
影响因子:
14.9
通讯作者:
Djinovic-Carugo K
Djinovic-Carugo K
中科院分区:
生物学2区
文献类型:
--
作者:
Beich-Frandsen M;Vecerek B;Konarev PV;Sjöblom B;Kloiber K;Hämmerle H;Rajkowitsch L;Miles AJ;Kontaxis G;Wallace BA;Svergun DI;Konrat R;Bläsi U;Djinovic-Carugo K

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The hexameric Escherichia coli RNA chaperone Hfq (HfqEc) 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 HfqEc. 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 HfqEc.
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