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Publication Detail
Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Sanders SL, Portoso M, Mata J, Bähler J, Allshire RC, Kouzarides T
  • Publication date:
    24/11/2004
  • Pagination:
    603, 614
  • Journal:
    Cell
  • Volume:
    119
  • Issue:
    5
  • Status:
    Published
  • Country:
    United States
  • Print ISSN:
    0092-8674
  • PII:
    S0092867404010530
  • Language:
    eng
  • Keywords:
    Cell Cycle Proteins, Cell Survival, DNA Damage, Gene Expression Regulation, Fungal, Genes, cdc, Histone-Lysine N-Methyltransferase, Histones, Intracellular Signaling Peptides and Proteins, Lysine, Methylation, Mutation, Nuclear Proteins, Phosphoproteins, Protein Methyltransferases, Protein Transport, Schizosaccharomyces, Schizosaccharomyces pombe Proteins
Abstract
Histone lysine methylation is a key regulator of gene expression and heterochromatin function, but little is known as to how this modification impinges on other chromatin activities. Here we demonstrate that a previously uncharacterized SET domain protein, Set9, is responsible for H4-K20 methylation in the fission yeast Schizosaccharomyces pombe. Surprisingly, H4-K20 methylation does not have any apparent role in the regulation of gene expression or heterochromatin function. Rather, we find the modification has a role in DNA damage response. Loss of Set9 activity or mutation of H4-K20 markedly impairs cell survival after genotoxic challenge and compromises the ability of cells to maintain checkpoint mediated cell cycle arrest. Genetic experiments link Set9 to Crb2, a homolog of the mammalian checkpoint protein 53BP1, and the enzyme is required for Crb2 localization to sites of DNA damage. These results argue that H4-K20 methylation functions as a "histone mark" required for the recruitment of the checkpoint protein Crb2.
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