The Bacillus subtilis RNA Helicase YxiN is Distended in Solution
Shuying Wang 1, Michael T Overgaard 1, YaoXiong Hu 1 and David B McKay 1*
1 Stanford University School of Medicine
* To whom correspondence should be addressed. E-mail: dave.mckay{at}stanford.edu.
Submitted on August 27, 2007
Revised on September 13, 2007
Accepted on 12 October 2007
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Abstract |
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The Bacillus subtilis YxiN protein is a modular three-domain RNA helicase of the DEx(D/H)-box protein family. The first two domains form the highly conserved "helicase core", and the third domain confers RNA target binding specificity. Small angle x-ray scattering on YxiN and two-domain fragments thereof shows that the protein has a distended structure in solution, in contrast to helicases involved in replication processes. These data are consistent with a "chaperone" activity in which the carboxy-terminal domain of YxiN tethers the protein to the vicinity of its targets and the helicase core is free to transiently interact with RNA duplexes, possibly to melt out misfolded elements of secondary structure.
Key Words:
Bacillus subtilis, RNA chaperone, RNA helicase, solution small-angle x-ray scattering
