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Elsevier, Biophysical Journal, 1(94), p. L01-L03, 2008

DOI: 10.1529/biophysj.107.120709

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The Bacillus subtilis RNA helicase YxiN is distended in solution.

Journal article published in 2008 by Shuying Wang, Michael Toft Overgaard ORCID, {Michael Toft} Overgaard, YaoXiong Hu, David B. McKay, {.-D. B.} McKay
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.