This Article Full Text Full Text (PDF) Supplement All Versions of this Article: biophysj.107.120709v1 94/1/L01    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Wang, S. Articles by McKay, D. B. Search for Related Content PubMed PubMed Citation Articles by Wang, S. Articles by McKay, D. B.

The Bacillus subtilis RNA Helicase YxiN is Distended in Solution

Department of Structural Biology, Stanford University School of Medicine, Stanford, California

Correspondence: Address reprint requests and inquiries to David B. McKay, E-mail: dave.mckay{at}stanford.edu.

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.