Direct interaction between Rsc6 and Rsc8/Swh3,two proteins that are conserved in SWI/SNF-related complexes.
Direct interaction between Rsc6 and Rsc8/Swh3,two proteins that are conserved in SWI/SNF-related complexes.
复制标题
Rsc6 和 Rsc8/Swh3（SWI/SNF 相关复合物中保守的两种蛋白质）之间的直接相互作用。
DOI：
10.1093/nar/26.16.3739
复制
发表时间：
1998
影响因子：
14.9
通讯作者：
Carlson,M
中科院分区：
文献类型：
--
作者：
Treich,I;Ho,L;Carlson,M
The RSC complex ofSaccharomyces cerevisiaeis closely related to the SWI/SNF complex. Both complexes are involved in remodeling chromatin structure and they share conserved components. The RSC proteins Sth1, Rsc8/Swh3, Sfh1 and Rsc6 are homologs of the SWI/SNF proteins Swi2/Snf2, Swi3, Snf5 and Swp73 respectively. To investigate the RSC complex, we isolated a temperature-sensitiveswh3allele. A screen for multicopy suppressors yielded plasmids carrying theRSC6andMAK31loci.RSC6also suppressed the formamide sensitivity of a strain with a C-terminal truncation ofSWH3. We show that Swh3 and Rsc6 fusion proteins interact in the two-hybrid system and that theswh3-tsmutation impairs this interaction. Finally, bacterially produced Swh3 and Rsc6 fusion proteins interactin vitro, supporting the genetic evidence for direct interaction between Swh3 and Rsc6in vivo. We have previously shown that Swh3 also interacts with Sth1. These findings, together with the conservation of these proteins in the SWI/SNF complex and in mammalian SWI/SNF-related complexes, strongly suggest that these proteins form a structural core for the complex.
