[an error occurred while processing this directive]

HEREDITAS ›› 2007, Vol. 29 ›› Issue (9): 1035-1035―1041.doi: 10.1360/yc-007-1035

• 综述 • Previous Articles     Next Articles

Progress in the study of histone methyltransferases

XIE Ping1, 2, TIAN Chun-Yan1, ZHANG Ling-Qiang1, AN Li-Guo2, HE Fu-Chu1

  

  1. 1. State Key Laboratory of Proteomics, Beijing Institute of Radiation Medicine, Beijing 100850, China
    2. College of Life Science, Shandong Normal University, Ji’nan 250014, China
  • Received:2007-02-14 Revised:2007-04-06 Online:2007-09-10 Published:2007-09-10

Abstract:

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.