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

Molecular cell | Apr 23, 2004

http://www.ncbi.nlm.nih.gov/pubmed/15099519

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 RIS Download

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

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM62970

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