Song Ji-Joon, Garlick Joseph D, Kingston Robert E
Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
Genes Dev. 2008 May 15;22(10):1313-8. doi: 10.1101/gad.1653308. Epub 2008 Apr 28.
p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a beta-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.
p55是许多染色质修饰复合物的常见组分,并且已被证明能与组蛋白结合。在此,我们展示了与组蛋白H4肽结合的果蝇p55的晶体结构。p55是一种预测的WD40重复蛋白,它通过位于β-螺旋桨结构一侧的结合口袋识别组蛋白H4的第一个螺旋。该口袋无法容纳H4的组蛋白折叠结构,H4的组蛋白折叠结构必须改变才能允许p55结合。重组实验表明,该结合口袋对含p55的复合物的功能很重要。这些数据证明,WD40重复蛋白利用各种表面来指导组蛋白的修饰。