title: Regulation of Transcription Factor Yin Yang 1 by SET7/9-mediated Lysine Methylation.
abstract: Yin Yang 1 (YY1) is a multifunctional transcription factor shown to be critical in a variety of biological processes. Although it is regulated by multiple types of post-translational modifications (PTMs), whether YY1 is methylated, which enzyme methylates YY1, and hence the functional significance of YY1 methylation remains completely unknown. Here we reported the first methyltransferase, SET7/9 (KMT7), capable of methylating YY1 at two highly conserved lysine (K) residues, K173 and K411, located in two distinct domains, one in the central glycine-rich region and the other in the very carboxyl-terminus. Functional studies revealed that SET7/9-mediated YY1 methylation regulated YY1 DNA-binding activity both in vitro and at specific genomic loci in cultured cells. Consistently, SET7/9-mediated YY1 methylation was shown to involve in YY1-regulated gene transcription and cell proliferation. Our findings revealed a novel regulatory strategy, methylation by lysine methyltransferase, imposed on YY1 protein, and linked YY1 methylation with its biological functions.
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Wen-juan
authors.initials: WJ
authors.lastname: Zhang
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Xiao-nan
authors.initials: XN
authors.lastname: Wu
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Tao-tao
authors.initials: TT
authors.lastname: Shi
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Huan-teng
authors.initials: HT
authors.lastname: Xu
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Jia
authors.initials: J
authors.lastname: Yi
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Hai-feng
authors.initials: HF
authors.lastname: Shen
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Ming-feng
authors.initials: MF
authors.lastname: Huang
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Xing-yi
authors.initials: XY
authors.lastname: Shu
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Fei-fei
authors.initials: FF
authors.lastname: Wang
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Bing-ling
authors.initials: BL
authors.lastname: Peng
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Rong-quan
authors.initials: RQ
authors.lastname: Xiao
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.|College of Chemistry and Chemical Engineering, Xiamen University, No. 422 Siming South Road, Xiamen, Fujian 361105, China.
authors.forename: Wei-wei
authors.initials: WW
authors.lastname: Gao
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Jian-cheng
authors.initials: JC
authors.lastname: Ding
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiang'an South Road, Xiamen, Fujian 361102, China.
authors.forename: Wen
authors.initials: W
authors.lastname: Liu
mesh_terms: D064113:CRISPR-Cas Systems; D049109:Cell Proliferation / Q000235:genetics; D057809:HEK293 Cells; D006367:HeLa Cells; D011495:Histone-Lysine N-Methyltransferase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D000072417:Protein Domains; D011499:Protein Processing, Post-Translational; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D014162:Transfection; D050986:YY1 Transcription Factor / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*
chemical_list: D034741:RNA, Small Interfering; D011994:Recombinant Proteins; D050986:YY1 Transcription Factor; C494698:YY1 protein, human; D011495:Histone-Lysine N-Methyltransferase; C540312:SETD7 protein, human; D008239:Lysine