Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3

• Published in: Biochemical and biophysical research communications 2013-01, Vol.430 (2), p.547-553
• Main Authors: Qin, Su, Guo, Yahong, Xu, Chao, Bian, Chuanbing, Fu, Minfei, Gong, Sarah, Min, Jinrong
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; DNA-Binding Proteins - chemistry; H3K36me3; Histones - chemistry; Humans; Methionine - chemistry; Molecular Sequence Data; MTF2; Nuclear Proteins - chemistry; PHF1; PHF19; Polycomb Repressive Complex 2 - chemistry; Polycomb-Group Proteins; PRC2; Protein Structure, Tertiary; Transcription Factors - chemistry; Tudor
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2012.11.116

► PHF1, MTF2 and PHF19 all contain a conserved Tudor domain. ► The Tudor domains of PCL proteins specifically recognized tri-methylated H3K36. ► The first PHD domains of PCL proteins do not display histone binding affinity. PRC2 is the major H3K27 methyltransferase and is responsible for maintaining repressed gene expression patterns throughout development. It contains four core components: EZH2, EED, SUZ12 and RbAp46/48 and some cell-type specific components. In this study, we focused on characterizing the histone binding domains of PHF1 and PHF19, and found that the Tudor domains of PHF1 and PHF19 selectively bind to histone H3K36me3. Structural analysis of these Tudor domains also shed light on how these Tudor domains selectively bind to histone H3K36me3. The histone H3K36me3 binding by the Tudor domains of PHF1, PHF19 and likely MTF2 provide another recruitment and regulatory mechanism for the PRC2 complex. In addition, we found that the first PHD domains of PHF1 and PHF19 do not exhibit histone H3K4 binding ability, nor do they affect the Tudor domain binding to histones.