{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nakamura R"],"funding":["KAKENHI","Takeda Science Foundation","Mochida Memorial Foundation for Medical and Pharmaceutical Research","JST","Uehara Memorial Foundation","The Japan Science Society","Ohsumi Frontier Science Foundation"],"pagination":["gkaf878"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12418378"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(17)"],"pubmed_abstract":["Methylation of histone H3 at lysine 9 (H3K9me), a hallmark of heterochromatin, is catalyzed by Clr4/Suv39. Clr4/Suv39 contains two conserved domains-an N-terminal chromodomain and a C-terminal catalytic domain-connected by an intrinsically disordered region (IDR). Several mechanisms have been proposed to regulate Clr4/Suv39 activity, but how it is regulated under physiological conditions remains largely unknown. We found that the N-terminus of Clr4 interacts with its C-terminal catalytic domain and represses its enzymatic activity. Detailed biochemical analyses revealed that basic amino acid residues in the IDR are involved in this interaction. Amino acid substitutions of these residues weakened this interaction, thereby promoting Clr4 activity in vitro. Interestingly, cells expressing mut"],"journal":["Nucleic acids research"],"pubmed_title":["Intrinsically disordered region of Clr4/Suv39 regulates its enzymatic activity and ensures heterochromatin spreading."],"pmcid":["PMC12418378"],"funding_grant_id":["JP23K27155","JPMJSP2104","JP24H02324","JP20H03189","JP18H05532","JP17H03713"],"pubmed_authors":["Nakagawa R","Yoshimura Y","Horikoshi N","Nakayama JI","Hayashi A","Nakamura R","Kurumizaka H"],"additional_accession":[]},"is_claimable":false,"name":"Intrinsically disordered region of Clr4/Suv39 regulates its enzymatic activity and ensures heterochromatin spreading.","description":"Methylation of histone H3 at lysine 9 (H3K9me), a hallmark of heterochromatin, is catalyzed by Clr4/Suv39. Clr4/Suv39 contains two conserved domains-an N-terminal chromodomain and a C-terminal catalytic domain-connected by an intrinsically disordered region (IDR). Several mechanisms have been proposed to regulate Clr4/Suv39 activity, but how it is regulated under physiological conditions remains largely unknown. We found that the N-terminus of Clr4 interacts with its C-terminal catalytic domain and represses its enzymatic activity. Detailed biochemical analyses revealed that basic amino acid residues in the IDR are involved in this interaction. Amino acid substitutions of these residues weakened this interaction, thereby promoting Clr4 activity in vitro. Interestingly, cells expressing mut","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-05-26T11:00:22.49Z","creation":"2026-05-24T03:07:33.429Z"},"accession":"S-EPMC12418378","cross_references":{"pubmed":["40923761"],"doi":["10.1093/nar/gkaf878"]}}