A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes.
A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes.
复制标题
SIN3L/RPD3L组蛋白脱乙酰基酶复合物的核心亚基内的帽帝型结构域与核酸G-四链体结合。
DOI：
10.1016/j.jbc.2021.101558
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发表时间：
2022-03
期刊：
影响因子：
--
通讯作者：
Radhakrishnan I
中科院分区：
文献类型：
--
作者：
Marcum RD;Hsieh J;Giljen M;Justice E;Daffern N;Zhang Y;Radhakrishnan I
含有组蛋白脱乙酰基酶（HDAC）活性在真核生物中的基因转录中起关键的作用Alian SIN3L/RPD3L复合物，包括十几个不同的多肽，这是一个古老的HDAC复合物，在这个复杂的港口保守的域名和未知的结构和功能的基序中，我们表明SDS3是一个组成型的，一个组成型的亚基，是Sin3L/rpd3l complex的正确功能ICAL TUDOR领域结合了修改的组织蛋白，SDS3限制了tudor域与核酸结合，可以形成高阶结构，例如G Quadruplexes，并与ESA1组蛋白乙酰基转移酶的打结的Tudor域共享相似之处，以前证明，该范围可显示单链rna的范围/r. rate rate rat rat rat rat res rat rat rat rat rat res rat。此HDAC复合物的角色。
Chromatin-modifying complexes containing histone deacetylase (HDAC) activities play critical roles in the regulation of gene transcription in eukaryotes. These complexes are thought to lack intrinsic DNA-binding activity, but according to a well-established paradigm, they are recruited via protein–protein interactions by gene-specific transcription factors and posttranslational histone modifications to their sites of action on the genome. The mammalian Sin3L/Rpd3L complex, comprising more than a dozen different polypeptides, is an ancient HDAC complex found in diverse eukaryotes. The subunits of this complex harbor conserved domains and motifs of unknown structure and function. Here, we show that Sds3, a constitutively-associated subunit critical for the proper functioning of the Sin3L/Rpd3L complex, harbors a type of Tudor domain that we designate the capped Tudor domain. Unlike canonical Tudor domains that bind modified histones, the Sds3 capped Tudor domain binds to nucleic acids that can form higher-order structures such as G-quadruplexes and shares similarities with the knotted Tudor domain of the Esa1 histone acetyltransferase that was previously shown to bind single-stranded RNA. Our findings expand the range of macromolecules capable of recruiting the Sin3L/Rpd3L complex and draw attention to potentially new biological roles for this HDAC complex.
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影响因子：
5.3
作者：
Guenther, MG;Barak, O;Lazar, MA
通讯作者：
Lazar, MA
DOI：
10.1016/j.bbagrm.2009.05.007
发表时间：
2009-06
期刊：
Biochimica et biophysica acta
影响因子：
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46.9
作者：
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通讯作者：
Drewes, Gerard
DOI：
10.1073/pnas.1418718112
发表时间：
2015-03-03
影响因子：
11.1
作者：
Chung, Wan Jun;Heddi, Brahim;Anh Tuan Phan
通讯作者：
Anh Tuan Phan