Crystal Structure of the C-Terminal Domain of Human DPY-30-Like Protein: A Component of the Histone Methyltransferase Complex
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- 作者：Xianping Wang ; Zhiyong Lou ; Xiuhua Dong ; Wen Yang ; Yong Peng ; Bin Yin ; Yanhua Gong ; Jiangang Yuan ; Weihong Zhou ; Mark Bartlam ; Xiaozhong Peng ; Zihe Rao
- 关键词：DPY-30L ; crystal structure ; dimer ; HMT complex ; X-type four helix bundle
- 刊名：Journal of Molecular Biology
- 出版年：2009
- 出版时间：17 July 2009
- 年：2009
- 卷：390
- 期：3
- 页码：530-537
- 全文大小：1685 K
文摘
The conserved DPY-30 is an essential component of the dosage compensation complex that balances the X-linked gene expression by regulation of the complex formation in Caenorhabditis elegans. The human DPY-30-like protein (DPY-30L) homolog is a conserved member of certain histone methyltransferase (HMT) complexes. In the human MLL1 (mixed-lineage leukemia-1) HMT complex, DPY-30L binds to the BRE2 homolog ASH2L in order to regulate histone 3–lysine 4 trimethylation. We have determined the 1.2-Å crystal structure of the human DPY-30L C-terminal domain (DPY-30LC). The DPY-30LC structure, harboring the conserved DPY-30 motif, is composed of two α-helices linked by a sharp loop and forms a typical X-type four-helix bundle required for dimer formation. DPY-30LC dimer formation is largely mediated by an extensive hydrophobic interface with some additional polar interactions. The oligomerization of DPY-30LC in solution, together with its reported binding to ASH2L, leads us to propose that the hydrophobic surface of the dimer may provide a platform for interaction with ASH2L in the MLL1 HMT complex.