Investigation of H2AX methylation by the SUV39H2 protein lysine methyltransferase

FEBS Lett. 2016 Jun;590(12):1713-9. doi: 10.1002/1873-3468.12216. Epub 2016 May 30.

Abstract

The H3K9 protein lysine methyltransferase SUV39H2 was reported to methylate K134 of H2AX and stimulate H2AX phosphorylation during DNA damage response [Sone K et al. (2014) Nat Commun 5, 5691]. However, the sequence context of H2AX-K134 differs from the specificity of SUV39H2. We performed in vitro methylation reactions with SUV39H2 (and its homolog SUV39H1) using H2AX protein and peptides, but no methylation at K134 or any other lysine in H2AX was detected. Positive controls demonstrated the functionality of the assays. While our data cannot finally exclude H2AX methylation of SUV39H2 in cells, additional experimental evidence is required to validate this claim.

Keywords: DNA repair; H2AX; SUV39H2; enzyme specificity; peptide recognition; protein lysine methylation.

MeSH terms

  • Histone-Lysine N-Methyltransferase / chemistry*
  • Histone-Lysine N-Methyltransferase / genetics
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / chemistry*
  • Histones / genetics
  • Histones / metabolism
  • Humans
  • Methylation
  • Substrate Specificity

Substances

  • H2AX protein, human
  • Histones
  • Histone-Lysine N-Methyltransferase
  • SUV39H2 protein, human

Associated data

  • GENBANK/BC011694