[Progress in the study of histone methyltransferases].
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.
Xie
Ping
P
State Key Laboratory of Proteomics, Beijing Institute of Radiation Medicine, Beijing 100850, China. xieping@hupo.org.cn
Tian
Chun-Yan
CY
Zhang
Ling-Qiang
LQ
An
Li-Guo
LG
He
Fu-Chu
FC
D002277:Carcinoma / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D008954:Models, Biological; D011496:Protein Methyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism
D006657:Histones; D016159:Tumor Suppressor Protein p53; D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase