HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription.

ABSTRACT: Increased histone acetylation has been correlated with increased transcription, and regions of heterochromatin are generally hypoacetylated. In investigating the cause-and-effect relationship between histone acetylation and gene activity, we have characterized two yeast histone deacetylase complexes. Histone deacetylase-A (HDA) is an approximately 350-kDa complex that is highly sensitive to the deacetylase inhibitor trichostatin A. Histone deacetylase-B (HDB) is an approximately 600-kDa complex that is much less sensitive to trichostatin A. The HDA1 protein (a subunit of the HDA activity) shares sequence similarity to RPD3, a factor required for optimal transcription of certain yeast genes. RPD3 is associated with the HDB activity. HDA1 also shares similarity to three new open reading fram

SUBMITTER: Rundlett SE 

PROVIDER: S-EPMC26162 | biostudies-literature | 1996 Dec

REPOSITORIES: biostudies-literature