HDA7 Background Information Remodeling of chromatin structure is believed to be a critical component of transcriptional regulation. A major source of remodeling is brought about by the acetylation of nucleosomal histones. Acetylation results in an allosteric change in the nucleosomal conformation and an increased accessibility of DNA to transcription factors. Conversely, the deacetylation of histones is associated with transcriptional silencing (1). HDA1, HDA2, HDA3, HDA4, HDA5, HDA6 and HDA7 have been identified as histone deacetylases in C. elegans and are homologous with histone deacetylase proteins in both yeast and mammalian systems (2,3). RBA1 and RBA2 are the C. elegans homologues of RbAp46 and RBAp48 respectively. RbAp46 and RbAp48 are Rb and histone binding proteins and are components of the histone deacetylase complex (4-6).
HDA7 (Ce-87)
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HDA7 (Ce-87): sc-5554. Western blot analysis of C. elegans recombinant HDA7 fusion protein.
