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The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly.

The yeast Hat1p/Hat2p type B histone acetyltransferase complex is localized to both the cytoplasm and nucleus. We isolate the nuclear form of the Hat1p/Hat2p complex and find that it copurifies with the product of the uncharacterized open reading frame YLL022C (named Hif1p). The functional significance of the association of Hif1p with the Hat1p/Hat2p complex is confirmed by the observation that hif1Delta and hat1Delta strains display similar defects in telomeric silencing and DNA double-strand break repair. Hif1p is a histone chaperone that selectively interacts with histones H3 and H4. Hif1p is also a chromatin assembly factor, promoting the deposition of histones in the presence of a yeast cytosolic extract. In vivo, the nuclear Hat1p/Hat2p/Hif1p complex is bound to acetylated histone H4, as well as histone H3. The association of Hif1p with acetylated H4 requires Hat1p and Hat2p providing a link between type B histone acetyltransferases and chromatin assembly.

Pubmed ID: 15099519


  • Ai X
  • Parthun MR


Molecular cell

Publication Data

April 23, 2004

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM62970

Mesh Terms

  • Acetyltransferases
  • Alleles
  • Blotting, Western
  • Cell Extracts
  • Cell Nucleus
  • Chromatin
  • Cytoplasm
  • DNA Damage
  • DNA Repair
  • DNA-Binding Proteins
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli
  • Fluorescent Antibody Technique, Indirect
  • Gene Deletion
  • Gene Silencing
  • Genes, Reporter
  • Histone Acetyltransferases
  • Hypoxia-Inducible Factor 1
  • Models, Molecular
  • Molecular Chaperones
  • Molecular Weight
  • Nuclear Proteins
  • Open Reading Frames
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Subcellular Fractions
  • Substrate Specificity
  • Telomere
  • Transcription Factors