title: Human ING1 proteins differentially regulate histone acetylation.
abstract: ING1 proteins are nuclear, growth inhibitory, and regulate apoptosis in different experimental systems. Here we show that similar to their yeast homologs, human ING1 proteins interact with proteins associated with histone acetyltransferase (HAT) activity, such as TRRAP, PCAF, CBP, and p300. Human ING1 immunocomplexes contain HAT activity, and overexpression of p33(ING1b), but not of p47(ING1a), induces hyperacetylation of histones H3 and H4, in vitro and in vivo at the single cell level. p47(ING1a) inhibits histone acetylation in vitro and in vivo and binds the histone deacetylase HDAC1. Finally, we present evidence indicating that p33(ING1b) affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300, an association that has been proposed to link DNA repair to chromatin remodeling. Together with the finding that human ING1 proteins bind PCNA in a DNA damage-dependent manner, these data suggest that ING1 proteins provide a direct linkage between DNA repair, apoptosis, and chromatin remodeling via multiple HAT.ING1.PCNA protein complexes.
authors.affiliation: Department of Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
authors.forename: Diego
authors.initials: D
authors.lastname: Vieyra
authors.forename: Robbie
authors.initials: R
authors.lastname: Loewith
authors.forename: Michelle
authors.initials: M
authors.lastname: Scott
authors.forename: Paul
authors.initials: P
authors.lastname: Bonnefin
authors.forename: Francois-Michel
authors.initials: FM
authors.lastname: Boisvert
authors.forename: Parneet
authors.initials: P
authors.lastname: Cheema
authors.forename: Svitlana
authors.initials: S
authors.lastname: Pastyryeva
authors.forename: Maria
authors.initials: M
authors.lastname: Meijer
authors.forename: Randal N
authors.initials: RN
authors.lastname: Johnston
authors.forename: David P
authors.initials: DP
authors.lastname: Bazett-Jones
authors.forename: Steven
authors.initials: S
authors.lastname: McMahon
authors.forename: Michael D
authors.initials: MD
authors.lastname: Cole
authors.forename: Dallan
authors.initials: D
authors.lastname: Young
authors.forename: Karl
authors.initials: K
authors.lastname: Riabowol
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D017209:Apoptosis / Q000502:physiology; D018797:Cell Cycle Proteins; D002460:Cell Line; D004268:DNA-Binding Proteins; D015536:Down-Regulation; D016147:Genes, Tumor Suppressor; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism*; D006801:Humans; D000076023:Inhibitor of Growth Protein 1; D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; D011506:Proteins / Q000378:metabolism* / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins; D025521:Tumor Suppressor Proteins
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D006657:Histones; C501503:ING1 protein, human; D000076023:Inhibitor of Growth Protein 1; D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D025521:Tumor Suppressor Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases