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Structural implications of Dpy30 oligomerization for MLL/SET1 COMPASS H3K4 trimethylation
  • 时间：0
  • 分类：Q523[生物学—生物化学] TM63[电气工程—电力系统及自动化]
  • 作者机构：[1]Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, [2]University of Chinese Academy of Sciences, Beijing 100049, China
  • 相关基金：We thank the staff of beamline 17U at the Shanghai Synchrotron Radiation Facility for technical support during data collection and Y. Y. Chen for help with the ITC assay. This work was supported by the National Natural Science Foundation of China （Grant Nos. 30900230 and 31021062） and the National Basic Research Pro- gram （973 Program） （No. 2011CBA00902）. Hongmei Zhang, Mei Li, Yu Gao, Chenjun Jia, Xiaowei Pan, Peng Cao, Xuelin Zhao, Jiping Zhang, and Wenrui Chang declare that they have no conflict of interest. This article does not contain any studies with human or animal subjects performed by the any of the authors.
作者： Hongmei Zhang[1], Mei Li[1], Yu Gao[1], Chenjun Jia[1,2], Xiaowei Pan[1], Peng Cao[1], Xuelin zhao[1], Jiping Zhang[1], Wenrui Chang[1]
关键词： COMPASS, 甲基化, 结构域, 齐聚, DNA修复, 蛋白复合物, 生物过程, 基因表达
中文摘要：

亲爱的编辑，

英文摘要：

Dear Editor, The methylation modifications of histone 3 lysine 4 （H3K4） have essential effects on biological processes including gene expression and transcription, cell cycle progression, and DNA repair. From yeast to mammals, the SET1 and MLL-like （mixed-lineage leukemia） multi-subunit protein complexes, known as SET1 or MLL COMPASS （Schneider et al., 2005）, are responsible for H3K4 methylation. In addition to the catalytic SET domain, the SET1 and MLL COMPASS complexes also contain a number of conserved subunits including WDR5 （Cps30）, RbBP5 （Cps50）.

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