期刊论文详细信息
JOURNAL OF MOLECULAR BIOLOGY 卷:404
Alternative Oligomeric States of the Yeast Rvb1/Rvb2 Complex Induced by Histidine Tags
Article
Cheung, Kevin L. Y.1,2  Huen, Jennifer3  Kakihara, Yoshito3  Houry, Walid A.3  Ortega, Joaquin1,2 
[1] McMaster Univ, Dept Biochem & Biomed Sci, Hamilton, ON L8N 3Z5, Canada
[2] McMaster Univ, MG DeGroote Inst Infect Dis Res, Hlth Sci Ctr, Hamilton, ON L8N 3Z5, Canada
[3] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
关键词: AAA;    electron microscopy;    helicase;    pontin;    reptin;   
DOI  :  10.1016/j.jmb.2010.10.003
来源: Elsevier
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【 摘 要 】

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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