对核小体重塑去乙酰化酶（NuRD）复合物结构的深入了解：RbAp48-MTA1亚复合物的结构
Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex.
作者信息
Alqarni Saad S M, Murthy Andal, Zhang Wei, Przewloka Marcin R, Silva Ana P G, Watson Aleksandra A, Lejon Sara, Pei Xue Y, Smits Arne H, Kloet Susan L, Wang Hongxin, Shepherd Nicholas E, Stokes Philippa H, Blobel Gerd A, Vermeulen Michiel, Glover David M, Mackay Joel P, Laue Ernest D
机构信息
From the School of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
出版信息
J Biol Chem. 2014 Aug 8;289(32):21844-55. doi: 10.1074/jbc.M114.558940. Epub 2014 Jun 11.
The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRD by determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.
核小体重塑与去乙酰化酶（NuRD）复合物是一种广泛保守的转录共调节因子，兼具核小体重塑和组蛋白去乙酰化活性。它在胚胎干细胞分化的早期阶段以及体细胞重编程为诱导多能干细胞的过程中发挥着关键作用。几种NuRD蛋白的异常与癌症和衰老相关。我们通过确定包含RbAp48和MTA1的亚复合物的结构来研究NuRD的结构。令人惊讶的是，RbAp48识别MTA1所使用的位点与其结合组蛋白H4所使用的位点相同，这表明组装进入NuRD会调节RbAp46/48与组蛋白的相互作用。结合其他结果，我们的数据表明MTA蛋白作为NuRD复合物组装的支架。我们进一步表明，RbAp48与MTA1的相互作用对于RbAp46/48在体内整合到NuRD复合物中至关重要。
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