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 (+2 others)
2002 Journal of Biological Chemistry  
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
more » ... 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 damagedependent manner, these data suggest that ING1 proteins provide a direct linkage between DNA repair, apoptosis, and chromatin remodeling via multiple HAT⅐ING1⅐PCNA protein complexes.
doi:10.1074/jbc.m200197200 pmid:12015309 fatcat:lqpyluugz5do7ovq47foixobku