Histone methyltransferase G9a contributes to H3K27 methylation in vivo

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2011,（2）
• 页码范围: 365-367
• 页数: 3页
• 语种: 英文
• DOI: 10.1038/cr.2010.157

摘要

Dear Editor, Histone modifications play a vital role in the conformation and function of their associated chromatin templates[1].Histone H3K27 methylation mediated by the PRC2 complex is critical for transcriptional regulation,Polycomb silencing,Drosophila segmentation,mammalian X inactivation and cancer[1].Interestingly,H3K27me1(H3 mono-methylated at residue K27)levels in vivo remain unaffected after PRC2 disruption[2,3],which is an indication for the existence of other contributing histone methyltransferase(s)to H3K27me1.