期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 404, 期 3, 页码 478-492出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.10.003
关键词
AAA; electron microscopy; helicase; pontin; reptin
资金
- National Science and Engineering Research Council of Canada [RGPIN288327-07]
- Canadian Institutes of Health Research [MOP-93778]
- Natural Sciences and Engineering Research Council of Canada
Rvb1 and Rvb2 are essential AAA(+) (ATPases associated with diverse cellular activities) helicases, which are important components of critical complexes such as chromatin remodeling and telomerase complexes. The oligomeric state of the Rvb proteins has been controversial. Independent studies from several groups have described the yeast and human Rvb1/Rvb2 complex both as a single and as a double hexameric ring complex. We found that histidine-tagged constructs of yeast Rvb proteins employed in some of these studies induced the assembly of double hexameric ring Rvb1/Rvb2 complexes. Instead, untagged versions of these proteins assemble into single hexameric rings. Furthermore, purified endogenous untagged Rvb1/Rvb2 complexes from Saccharomyces cerevisiae were also found as single hexameric rings, similar to the complexes assembled in vitro from the purified untagged components. These results demonstrate that some of the differences between the reported structures are caused by histidine tags and imply that further studies on the purified proteins should be carried out using untagged constructs. (c) 2010 Elsevier Ltd. All rights reserved.
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