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您的检索式：作者名="Shuailong Han"
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| 1 | Structural basis for nucleosome binding and catalysis by the yeast Rpd3S/HDAC holoenzyme显示文摘Dear Editor,Histone deacetylases(HDACs)are evolutionally conserved enzymes that remove acetyl modifications from histones and play a central role in epigenetic gene silencing.1 Class I HDACs are promising targets for epigenetic therapies for a range of diseases such as cancers,inflammations,infections,and neurological diseases.2 Yeast Rpd3 is the founding member of class I HDACs,which forms two distinct complexes:the∼1.2 MDa Rpd3L deacetylating histones at promoter regions,and the∼0.6 MDa Rpd3S targeting transcribed regions to suppress intragenic transcription initiation.3,4 Rpd3S consists of three core proteins:Rpd3,Sin3,and Ume15 along with two dedicated chromatin binding subunits:Eaf3 and Rco1.6 The structures of the yeast Rpd3S complex and its human homolog Sin3B complex have been recently reported.7,8 Here,we report the cryo-electron microscopy(cryo-EM)structure of the Rpd3S holoenzyme binding a nucleosome at 3.7Åresolution(Supplementary information,Table S1). | Yueyue Zhang Mengxue Xu Po Wang Jiahui Zhou Guangxian Wang Shuailong Han Gang Cai Xuejuan Wang | 2023 | Cell Research2023，33，12： | 0 |
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