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Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex.
Cell Reports ( IF 7.5 ) Pub Date : 2020-02-25 , DOI: 10.1016/j.celrep.2020.01.091
Yun Song 1 , Lisbeth Dagil 2 , Louise Fairall 1 , Naomi Robertson 3 , Mingxuan Wu 4 , T J Ragan 1 , Christos G Savva 1 , Almutasem Saleh 1 , Nobuhiro Morone 5 , Micha B A Kunze 2 , Andrew G Jamieson 3 , Philip A Cole 4 , D Flemming Hansen 2 , John W R Schwabe 1
Affiliation  

The transcriptional corepressor complex CoREST is one of seven histone deacetylase complexes that regulate the genome through controlling chromatin acetylation. The CoREST complex is unique in containing both histone demethylase and deacetylase enzymes, LSD1 and HDAC1, held together by the RCOR1 scaffold protein. To date, it has been assumed that the enzymes function independently within the complex. Now, we report the assembly of the ternary complex. Using both structural and functional studies, we show that the activity of the two enzymes is closely coupled and that the complex can exist in at least two distinct states with different kinetics. Electron microscopy of the complex reveals a bi-lobed structure with LSD1 and HDAC1 enzymes at opposite ends of the complex. The structure of CoREST in complex with a nucleosome reveals a mode of chromatin engagement that contrasts with previous models.

中文翻译:

CoREST 复合物中 LSD1 去甲基化酶和 HDAC1 去乙酰化酶之间的串扰机制。

转录辅阻遏复合物 CoREST 是七种组蛋白去乙酰化酶复合物之一,通过控制染色质乙酰化来调节基因组。CoREST 复合物的独特之处在于同时包含组蛋白去甲基化酶和去乙酰化酶 LSD1 和 HDAC1,它们由 RCOR1 支架蛋白结合在一起。迄今为止,已假定酶在复合物中独立发挥作用。现在,我们报告三元复合体的组装。使用结构和功能研究,我们表明这两种酶的活性是紧密耦合的,并且复合物可以以至少两种不同的状态存在,具有不同的动力学。复合物的电子显微镜显示在复合物的两端具有 LSD1 和 HDAC1 酶的双叶结构。
更新日期:2020-02-25
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