识别和描述的三个新组件mSin3A辅阻遏物复杂。
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弗莱舍TC、云UJ艾耶尔德
识别和描述的三个新组件mSin3A辅阻遏物复杂。
摩尔细胞杂志。2003;23 (10):3456 - 67。
- PubMed ID
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12724404 (在PubMed]
- 文摘
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复杂的mSin3A辅阻遏物包含7到10紧密相关的多肽和利用许多转录阻遏物。大部分mSin3A来自协会的辅阻遏物功能和组蛋白去乙酰酶抑制剂HDAC1 HDAC2;然而,其他的贡献mSin3A-associated多肽在很大程度上仍未知。我们有净化的mSin3A复杂K562白血病细胞和确认三个新mSin3A-associated蛋白质(SAP): SAP180 SAP130, SAP45。SAP180相同之前确定mSin3A-associated蛋白质40%,RBP1。SAP45 mSDS3相同,人类直接同源SDS3p组件的酿酒酵母Sin3p-Rpd3p辅阻遏物复杂。SAP130没有检测到其他蛋白质同源性。Coimmunoprecipitation和凝胶过滤数据表明,新削弱了,至少,组件相同的mSin3A复杂。每一个新的SAP压抑拴在DNA转录。此外,镇压与mSin3A绑定,这表明新削弱了组件功能mSin3A辅阻遏物复合物。 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.