Histone deacetylase activity is required for full transcriptional repression by mSin3A
Histone deacetylase activity is required for full transcriptional repression by mSin3A
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DOI：
10.1016/s0092-8674(00)80214-7
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发表时间：
1997-05-02
期刊：
影响因子：
64.5
通讯作者：
Ayer, DE
中科院分区：
文献类型：
--
作者：
Hassig, CA;Fleischer, TC;Ayer, DE
bHLH-Zip蛋白的Mad家族成员与Max异源二聚化，以序列特异性方式抑制转录。Mad：Max异源二聚体的转录抑制是通过与辅阻遏物mSin 3A或mSin 3B形成三元复合物来介导的。我们在这里报告说，mSin 3A是一个大的，异质性的多蛋白复合物的体内组件，并紧密和具体地与至少七个多肽。两种mSin 3A相关蛋白，p50和p55，与组蛋白去乙酰化酶HDAC 1高度相关。mSin 3A免疫复合物具有对特异性脱乙酰酶抑制剂trapoxin敏感的组蛋白脱乙酰酶活性。通过trapoxin处理减少了报告基因的mSin 3A靶向抑制，表明组蛋白脱乙酰化通过Mad-Max-mSin 3A多聚体复合物介导转录抑制。
Members of the Mad family of bHLH-Zip proteins heterodimerize with Max to repress transcription in a sequence-specific manner. Transcriptional repression by Mad:Max heterodimers is mediated by ternary complex formation with either of the corepressors mSin3A or mSin3B. We report here that mSin3A is an in vivo component of large, heterogeneous multiprotein complexes and is tightly and specifically associated with at least seven polypeptides. Two of the mSin3A-associated proteins, p50 and p55, are highly related to the histone deacetylase HDAC1. The mSin3A immunecomplexes possess histone deacetylase activity that is sensitive to the specific deacetylase inhibitor trapoxin. mSin3A-targeted repression of a reporter gene is reduced by trapoxin treatment, suggesting that histone deacetylation mediates transcriptional repression through Mad-Max-mSin3A multimeric complexes.