Abstract:
Histone deacetylases are integral components of transcriptionally repressive complexes. The substrates for such complexes containing human HDAC1, HDAC2, and HDAC3 have not been identified. We examined the ability of these complexes to deacetylate total free histones, individual core histones, H2A-H2B dimers, H3-H4 tetramers, polynucleosomes, mononucleosomes, and non-histone substrates. We also identified several complexes which utilize HDAC towards transcriptional repression. The regulation of HDAC activity was also investigated. In particular, we found that a phosphorylation event influences HDAC activity. Addition of phosphatase inhibitors alone greatly increases HDAC activity. The predominant chicken immature erythrocyte histone deacetylase is cHDAC1, the hHDAC1 homolog. We investigated the possibility that another form of HDAC exists in these cells. (Abstract shortened by UMI.)
