Journal
BIOPHYSICAL JOURNAL
Volume 94, Issue 1, Pages L1-L3Publisher
BIOPHYSICAL SOC
DOI: 10.1529/biophysj.107.120709
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM071696] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM071696, GM-71696] Funding Source: Medline
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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.
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