title: H3K27 demethylases, at long last.
abstract: Methylation of lysine 27 on histone H3 (H3K27me) by the Polycomb complex (PRC2) proteins is associated with gene silencing in many developmental processes. A cluster of recent papers (Agger et al., 2007; De Santa et al., 2007; Lan et al., 2007; Lee et al., 2007) identify the JmjC-domain proteins UTX and JMJD3 as H3K27-specific demethylases that remove this methyl mark, enabling the activation of genes involved in animal body patterning and the inflammatory response.
authors.affiliation: Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors.forename: Tomek
authors.initials: T
authors.lastname: Swigut
authors.forename: Joanna
authors.initials: J
authors.lastname: Wysocka
mesh_terms: D000818:Animals; D019521:Body Patterning; D044127:Epigenesis, Genetic; D005786:Gene Expression Regulation; D020868:Gene Silencing; D018398:Homeodomain Proteins / Q000235:genetics / Q000378:metabolism; D007107:Immune System / Q000502:physiology; D056484:Jumonji Domain-Containing Histone Demethylases; D008745:Methylation; D010089:Oxidoreductases, N-Demethylating / Q000235:genetics / Q000378:metabolism*; D063146:Polycomb-Group Proteins; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D018398:Homeodomain Proteins; D063146:Polycomb-Group Proteins; D012097:Repressor Proteins; D056484:Jumonji Domain-Containing Histone Demethylases; C523761:Kdm6b protein, mouse; D010089:Oxidoreductases, N-Demethylating