Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex

被引：4
作者：
Clark, Michael David [1 ]
Zhang, Yongbo [2 ]
Radhakrishnan, Ishwar [1 ]
机构：
[1] Northwestern Univ, Dept Mol Biosci, Evanston, IL 60208 USA
[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
来源：
JOURNAL OF MOLECULAR BIOLOGY | 2015年 / 427卷 / 24期
关键词：
conformational exchange; conformational heterogeneity; multiple binding modes; NMR spectroscopy; protein-protein interaction; TRANSCRIPTIONAL REPRESSION; SPECTROSCOPY; COMPONENT; DYNAMICS; BINDING; STATES;
D O I：
10.1016/j.jmb.2015.10.018
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The Sds3 transcriptional corepressor facilitates the assembly of the 1- to 2-MDa histone deacetylase-associated Sin3L/Rpd3L complex by providing a crucial homodimerization activity. Sds3 engages the scaffolding protein Sin3A, via a bipartite motif within the Sin3 interaction domain (SID) comprising a helix and an extended segment. Here, we show that the SID samples two discrete, substantially populated conformations with lifetimes in the tens of milliseconds range. The two conformations differ via a translation of the main chain and the corresponding side chains in the 5- to 7-angstrom range. Given the close proximity of the SID to other functional motifs in Sds3 at the sequence level, the conformational exchange has the potential to regulate these activities. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码：3817 / 3823
页数：7
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