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Human ING1 proteins differentially regulate histone acetylation.

Diego Vieyra·Robbie Loewith·Michelle Scott·Paul Bonnefin·Francois-Michel Boisvert·Parneet Cheema·Svitlana Pastyryeva·Maria Meijer·Randal N Johnston·David P Bazett-Jones·Steven McMahon·Michael D Cole·Dallan Young·Karl Riabowol
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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.

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AcetylationAcetyltransferasesApoptosisCell Cycle ProteinsCell LineDNA-Binding ProteinsDown-RegulationGenes, Tumor SuppressorHistone AcetyltransferasesHistonesHumansInhibitor of Growth Protein 1Intracellular Signaling Peptides and ProteinsNuclear ProteinsProteinsSaccharomyces cerevisiae ProteinsTumor Suppressor ProteinsJournal ArticleResearch Support, Non-U.S. Gov't

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Diego Vieyra, Robbie Loewith, Michelle Scott, Paul Bonnefin, Francois-Michel Boisvert, Parneet Cheema, Svitlana Pastyryeva, Maria Meijer, Randal N Johnston, David P Bazett-Jones, Steven McMahon, Michael D Cole, Dallan Young, Karl Riabowol. 2002-05-15. Human ING1 proteins differentially regulate histone acetylation.. https://doi.org/10.1074/jbc.m200197200

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