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首页> 外文期刊>Molecular and Cellular Biology >Identification and Characterization of Three New Components of the mSin3A Corepressor Complex
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Identification and Characterization of Three New Components of the mSin3A Corepressor Complex

机译：mSin3A Corepressor复合体的三个新成分的鉴定和表征

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The mSin3A corepressor complex contains 7 to 10 tightly associated polypeptides and is utilized by many transcriptional repressors. Much of the corepressor function of mSin3A derives from associations with the histone deacetylases HDAC1 and HDAC2; however, the contributions of the other mSin3A-associated polypeptides remain largely unknown. We have purified an mSin3A complex from K562 erythroleukemia cells and identified three new mSin3A-associated proteins (SAP): SAP180, SAP130, and SAP45. SAP180 is 40% identical to a previously identified mSin3A-associated protein, RBP1. SAP45 is identical to mSDS3, the human ortholog of the SDS3p component of the Saccharomyces cerevisiae Sin3p-Rpd3p corepressor complex. SAP130 does not have detectable homology to other proteins. Coimmunoprecipitation and gel filtration data suggest that the new SAPs are, at the very least, components of the same mSin3A complex. Each new SAP repressed transcription when tethered to DNA. Furthermore, repression correlated with mSin3A binding, suggesting that the new SAPs are components of functional mSin3A corepressor complexes. SAP180 has two repression domains: a C-terminal domain, which interacts with the mSin3A-HDAC complex, and an N-terminal domain, which functions independently of mSin3A-HDAC. SAP130 has a repression domain at its C terminus that interacts with the mSin3A-HDAC complex and an N-terminal domain that probably mediates an interaction with a transcriptional activator. Together, our data suggest that these novel SAPs function in the assembly and/or enzymatic activity of the mSin3A complex or in mediating interactions between the mSin3A complex and other regulatory complexes. Finally, all three SAPs bind to the HDAC-interaction domain (HID) of mSin3A, suggesting that the HID functions as the assembly interface for the mSin3A corepressor complex.
机译：mSin3A共抑制物复合物包含7至10个紧密相关的多肽，并被许多转录抑制物利用。 mSin3A的许多核心表达功能均来自与组蛋白脱乙酰基酶HDAC1和HDAC2的缔合。然而，其他与mSin3A相关的多肽的贡献仍然未知。我们已经从K562红白血病细胞中纯化了mSin3A复合物，并鉴定了三种新的与mSin3A相关的蛋白质（SAP）：SAP180，SAP130和SAP45。 SAP180与先前鉴定的mSin3A相关蛋白RBP1 40％相同。 SAP45与mSDS3相同，mSDS3是酿酒酵母Sin3p-Rpd3p核心复合物的SDS3p成分的人类直系同源物。 SAP130与其他蛋白质没有可检测的同源性。免疫共沉淀和凝胶过滤数据表明，新的SAP至少是同一mSin3A复合物的组成部分。每个新的SAP束缚到DNA时都会抑制转录。此外，抑制与mSin3A结合相关，这表明新的SAP是功能性mSin3A心脏加压复合物的组成部分。 SAP180具有两个抑制域：一个与mSin3A-HDAC复合体相互作用的C末端域，一个与mSin3A-HDAC独立起作用的N末端域。 SAP130在其C末端具有一个与mSin3A-HDAC复合体相互作用的阻抑域，一个N末端域可能介导了与转录激活因子的相互作用。在一起，我们的数据表明，这些新型的SAP在mSin3A复合体的组装和/或酶促活性中或在mSin3A复合体与其他调控复合体之间的介导相互作用中起作用。最后，所有这三个SAP都绑定到mSin3A的HDAC交互域（HID），这表明该HID充当mSin3A共压复合物的组装接口。

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