Xie Ping, Tian Chun-Yan, Zhang Ling-Qiang, An Li-Guo, He Fu-Chu
State Key Laboratory of Proteomics, Beijing Institute of Radiation Medicine, Beijing 100850, China.
Yi Chuan. 2007 Sep;29(9):1035-41. doi: 10.1360/yc-007-1035.
Site- and state-specific lysine methylation of histones is catalyzed by a family of proteins including those contain the evolutionarily conserved SET domain. Research on histone methyltransferases is a part of epigenetics, which plays a fundamental role in heterochromatin formation, X-chromosome inactivation and transcription regulation. Aberrant histone methylation was linked to a number of developmental disorders and human disease including several carcinomas. Histone lysine methylation is a functionally complex process, as it can either activate or repress transcription, depending on sequence-specific lysine methylation site in histones. Non-histone proteins were found to be methylated by SET domain-containing histone methyltransferases whose primary targets were presumed to be histones. The researches on histone methyltransferases will make a completely new space for transcriptional activity, embryonic development, cell differentiation, and signal transduction.
组蛋白位点和状态特异性赖氨酸甲基化由包括那些含有进化保守SET结构域的蛋白质家族催化。对组蛋白甲基转移酶的研究是表观遗传学的一部分,表观遗传学在异染色质形成、X染色体失活和转录调控中起基本作用。异常的组蛋白甲基化与许多发育障碍和人类疾病有关,包括几种癌症。组蛋白赖氨酸甲基化是一个功能复杂的过程,因为它可以激活或抑制转录,这取决于组蛋白中序列特异性赖氨酸甲基化位点。发现非组蛋白蛋白质可被含SET结构域的组蛋白甲基转移酶甲基化,其主要靶标被认为是组蛋白。对组蛋白甲基转移酶的研究将为转录活性、胚胎发育、细胞分化和信号转导开辟全新的空间。