Crystal structure of the C-terminal domain of human DPY-30-like protein: A component of the histone methyltransferase complex.

Xianping Wang, Zhiyong Lou, Xiuhua Dong, Wen Yang, Yong Peng, Bin Yin, Yanhua Gong, Jiangang Yuan, Weihong Zhou, Mark Bartlam, Xiaozhong Peng, Zihe Rao

Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences/Peking Union Medical College, Beijing, China.

Journal of molecular biology 2009 Jul 17

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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-A crystal structure of the human DPY-30L C-terminal domain (DPY-30L(C)). The DPY-30L(C) structure, harboring the conserved DPY-30 motif, is composed of two alpha-helices linked by a sharp loop and forms a typical X-type four-helix bundle required for dimer formation. DPY-30L(C) dimer formation is largely mediated by an extensive hydrophobic interface with some additional polar interactions. The oligomerization of DPY-30L(C) 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.

Citation

Xianping Wang, Zhiyong Lou, Xiuhua Dong, Wen Yang, Yong Peng, Bin Yin, Yanhua Gong, Jiangang Yuan, Weihong Zhou, Mark Bartlam, Xiaozhong Peng, Zihe Rao. Crystal structure of the C-terminal domain of human DPY-30-like protein: A component of the histone methyltransferase complex. Journal of molecular biology. 2009 Jul 17;390(3):530-7