Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
复制标题
组蛋白脱乙酰酶相关 Sin3L/Rpd3L 辅阻遏物复合体中 Sds3 亚基与 Sin3 接合的替代模式的溶液 NMR 研究。
DOI：
10.1016/j.jmb.2015.10.018
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发表时间：
2015
影响因子：
5.6
通讯作者：
Radhakrishnan,Ishwar
中科院分区：
文献类型：
--
作者：
Clark,MichaelDavid;Zhang,Yongbo;Radhakrishnan,Ishwar
Sds 3转录辅阻遏物通过提供关键的同源二聚化活性促进1-至2-MDa组蛋白脱乙酰酶相关的Sin 3L/Rpd 3L复合物的组装。Sds 3通过包含螺旋和延伸片段的Sin 3相互作用结构域（SID）内的二分基序接合支架蛋白Sin 3A。在这里，我们表明，SID采样两个离散的，基本上填充构象的寿命在几十毫秒的范围内。这两种构象的不同之处在于主链和相应的侧链在5-至7-π范围内的平移。由于SID在序列水平上与Sds 3中的其他功能基序非常接近，构象交换具有调节这些活动的潜力。
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-Å 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.
影响因子：
6.1
作者：
Anthis NJ;Clore GM
通讯作者：
Clore GM
DOI：
10.1016/j.bbaexp.2005.09.005
发表时间：
2005-11-10
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
影响因子：
--
作者：
Carrozza, MJ;Florens, L;Workman, JL
通讯作者：
Workman, JL
DOI：
10.1016/j.bbapap.2010.10.012
发表时间：
2011-08
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Kleckner IR;Foster MP
通讯作者：
Foster MP