Nucleic Acids Research Advance Access originally published online on December 2, 2008
Nucleic Acids Research 2009 37(2):421-430; doi:10.1093/nar/gkn947
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Nucleic Acids Research, 2009, Vol. 37, No. 2 421-430
© 2008 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 |
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility
1Division of Biophysical Chemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland and 2Department of Molecular Structural Biology, University of Göttingen, D-37077 Göttingen, Germany
*To whom correspondence should be addressed. Tel: +41 61 267 23 81; Fax: +41 61 267 21 89; Email: dagmar.klostermeier{at}unibas.ch
Received September 23, 2008. Revised October 30, 2008. Accepted November 8, 2008.
DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.
The coordinates and structure factors have been deposited in the Protein Data Bank (accession codes 3eaq, 3ear and 3eas).
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  M. G. Rudolph and D. Klostermeier The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core RNA, November 1, 2009; 15(11): 1993 - 2001. [Abstract] [Full Text] [PDF]
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