title: Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.
abstract: Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger-containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide.
authors.affiliation: MRC Centre for Protein Engineering, Cambridge, UK.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Vezzoli
authors.forename: Nicolas
authors.initials: N
authors.lastname: Bonadies
authors.forename: Mark D
authors.initials: MD
authors.lastname: Allen
authors.forename: Stefan M V
authors.initials: SM
authors.lastname: Freund
authors.forename: Clara M
authors.initials: CM
authors.lastname: Santiveri
authors.forename: Brynn T
authors.initials: BT
authors.lastname: Kvinlaug
authors.forename: Brian J P
authors.initials: BJ
authors.lastname: Huntly
authors.forename: Berthold
authors.initials: B
authors.lastname: Göttgens
authors.forename: Mark
authors.initials: M
authors.lastname: Bycroft
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D000092468:Bromodomain Containing Proteins
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D004268:DNA-Binding Proteins; D006657:Histones; D009687:Nuclear Proteins; C086011:BRPF1 protein, human; D000092468:Bromodomain Containing Proteins
references.citation: Nature. 2009 Jul 9;460(7252):287-91
references.pmid: 19483677
references.citation: Oncogene. 2007 Aug 13;26(37):5408-19
references.pmid: 17694082
references.citation: J Mol Biol. 2003 Jul 11;330(3):571-6
references.pmid: 12842472
references.citation: Proc Natl Acad Sci U S A. 2009 Feb 10;106(6):1886-91
references.pmid: 19181860
references.citation: Science. 2007 May 18;316(5827):1050-4
references.pmid: 17510366
references.citation: Development. 2008 Jun;135(11):1935-46
references.pmid: 18469222
references.citation: FEBS Lett. 2000 May 4;473(1):1-5
references.pmid: 10802047
references.citation: Nat Rev Mol Cell Biol. 2007 Dec;8(12):983-94
references.pmid: 18037899
references.citation: Mutat Res. 2007 May 1;618(1-2):130-4
references.pmid: 17346757
references.citation: Trends Biotechnol. 2006 Jan;24(1):22-7
references.pmid: 16216358
references.citation: Mol Cell. 2009 Feb 27;33(4):428-37
references.pmid: 19250904
references.citation: J Biol Chem. 2003 Nov 21;278(47):46968-73
references.pmid: 12952983
references.citation: Cancer Cell. 2004 Dec;6(6):587-96
references.pmid: 15607963
references.citation: Mol Cell Biol. 2008 Nov;28(22):6828-43
references.pmid: 18794358
references.citation: Trends Biochem Sci. 2003 Feb;28(2):69-74
references.pmid: 12575993
references.citation: Nat Struct Biol. 2002 Mar;9(3):217-24
references.pmid: 11836534
references.citation: Nat Cell Biol. 2007 Jul;9(7):804-12
references.pmid: 17589499
references.citation: Cell. 2007 May 18;129(4):823-37
references.pmid: 17512414
references.citation: Nat Genet. 2009 Mar;41(3):376-81
references.pmid: 19182803
references.citation: Nat Struct Mol Biol. 2007 Nov;14(11):1025-1040
references.pmid: 17984965