HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1

Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4391-6. doi: 10.1073/pnas.081560698. Epub 2001 Apr 3.

Abstract

Histone deacetylase HDA1, the prototype for the class II mammalian deacetylases, is likely the catalytic subunit of the HDA1-containing complex that is involved in TUP1-specific repression and global deacetylation in yeast. Although the class I RPD3-like enzymatic complexes have been well characterized, little is known about the identity and interactions of the factors that associate to form the HDA1 complex. In this paper, we identify related HDA2 and HDA3 proteins that are found in the HDA1 complex and show that HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a likely tetramer. These interactions are necessary for catalytic activity because mutations in any of the three components disrupt activity both in vitro and in vivo. In this respect the HDA1 complex differs from yeast RPD3, which has components such as SIN3 that are not essential for activity in vitro, and yeast HOS3, which has intrinsic in vitro activity as a homodimer in the absence of other subunits.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Base Sequence
  • Cation Transport Proteins*
  • DNA Primers
  • Histone Deacetylases / metabolism*
  • Isoenzymes / metabolism*
  • Precipitin Tests
  • Promoter Regions, Genetic
  • Protein Binding
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins*
  • Sodium-Potassium-Exchanging ATPase

Substances

  • Cation Transport Proteins
  • DNA Primers
  • ENA1 protein, S cerevisiae
  • Isoenzymes
  • Saccharomyces cerevisiae Proteins
  • Histone Deacetylases
  • Adenosine Triphosphatases
  • Sodium-Potassium-Exchanging ATPase