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Nuclear Hat1p complex (NuB4) components participate in DNA repair-linked chromatin reassembly.

Chromatin is disassembled and reassembled during DNA repair. To assay chromatin reassembly accompanying DNA double strand break repair, ChIP analysis can be used to monitor the presence of histone H3 near the lesion. The chromatin assembly factor Asf1p, as well as the acetylation of histone H3 lysine 56, have been shown to promote chromatin reassembly when DNA double strand break repair is complete. Using Gal-HO-mediated double strand break repair, we have tested each of the components of the nuclear Hat1p-containing type B histone acetyltransferase complex (NuB4) and have found that they can affect repair-linked chromatin reassembly but that their contributions are not equivalent. In particular, deletion of the catalytic subunit, Hat1p, caused a significant defect in chromatin reassembly. In addition, loss of the histone chaperone Hif1p, when combined with an allele of H3 that mutates lysines 14 and 23 to arginine, has a pronounced effect on chromatin reassembly that is similar to that observed in an asf1Δ. The role of Hat1p and Hif1p is at least partially redundant with the role of Asf1p. Consistent with a more prominent role for Hif1p in chromatin reassembly than either Hat1p or Hat2p, Hif1p exists in complex(es) independent of Hat1p and Hat2p and influences the activity of an H3-specific histone acetyltransferase activity. Our data directly demonstrate the role of the nuclear HAT1 complex (NuB4) components in DNA repair-linked chromatin reassembly.

Pubmed ID: 21454479


  • Ge Z
  • Wang H
  • Parthun MR


The Journal of biological chemistry

Publication Data

May 13, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM62970
  • Agency: NIGMS NIH HHS, Id: R01 GM062970

Mesh Terms

  • Acetylation
  • Alleles
  • Catalysis
  • Cell Nucleus
  • Chromatin
  • Chromatin Immunoprecipitation
  • DNA Damage
  • DNA Repair
  • Endonucleases
  • Histone Acetyltransferases
  • Histone Chaperones
  • Histones
  • Nuclear Proteins
  • Protein Binding
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins