PHD finger of the SUMP ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2
PHD finger of the SUMP ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2
复制标题
水稻中 SUMP 连接酶 Siz/PIAS 家族的 PHD 手指揭示了甲基化组蛋白 H3 在赖氨酸 4 和精氨酸 2 处的特异性结合
DOI：
10.1016/j.febslet.2012.04.063
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发表时间：
2012
期刊：
影响因子：
3.5
通讯作者：
T. Yamazaki
中科院分区：
文献类型：
--
作者：
H. Shindo;R. Suzuki;W. Tsuchiya;M. Taichi;Y. Nishiuchi;T. Yamazaki
我们通过核磁共振波谱确定了水稻Siz/PIAS型SUMO连接酶OsSiz 1的PHD指的三维结构，并研究了其与多种甲基化组蛋白H3尾部的结合能力，结果表明OsSiz 1-PHD主要识别组蛋白H3的二甲基化Arg 2，Arg 2和Lys 4的甲基化对OsSiz 1-PHD的结合具有协同效应。OsSiz 1-PHD对H3 K4 me 3的三甲基化Lys 4的K4笼与BPTF-PHD指的K4笼相似，而对Arg 2的R2口袋不同。令人感兴趣的是，Siz/皮亚斯的PHD模块与DNA结合结构域SAP协作，通过与甲基化的富含精氨酸的染色质结构域相关的多种效应物的SUMO化在基因调控中起重要作用。
We determined the three-dimensional structure of the PHD finger of the rice Siz/PIAS-type SUMO ligase, OsSiz1, by NMR spectroscopy and investigated binding ability for a variety of methylated histone H3 tails, showing that OsSiz1–PHD primarily recognizes dimethylated Arg2 of the histone H3 and that methylations at Arg2 and Lys4 reveal synergy effect on binding to OsSiz1–PHD. The K4 cage of OsSiz1–PHD for trimethylated Lys4 of H3K4me3 was similar to that of the BPTF–PHD finger, while the R2 pocket for Arg2 was different. It is intriguing that the PHD module of Siz/PIAS plays an important role, with collaboration with the DNA binding domain SAP, in gene regulation through SUMOylation of a variety of effectors associated with the methylated arginine-riched chromatin domains.