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dc.contributor.author Moniwa, Mariko en_US
dc.date.accessioned 2007-07-12T17:47:31Z
dc.date.available 2007-07-12T17:47:31Z
dc.date.issued 2000-08-01T00:00:00Z en_US
dc.identifier.uri http://hdl.handle.net/1993/2514
dc.description.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.) en_US
dc.format.extent 6123809 bytes
dc.format.extent 184 bytes
dc.format.mimetype application/pdf
dc.format.mimetype text/plain
dc.language en en_US
dc.language.iso en_US
dc.title Characterization of the human HDAC1, HDAC2, HDAC3, and chicken erythrocyte histone deacetylase activities en_US
dc.degree.discipline Biochemistry & Medical Genetics en_US
dc.degree.level Master of Science (M.Sc.) en_US


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