Local generation of fumarate promotes DNA repair through inhibition of histone H3 demethylation

Nat Cell Biol. 2015 Sep;17(9):1158-68. doi: 10.1038/ncb3209. Epub 2015 Aug 3.

Abstract

Histone methylation regulates DNA repair. However, the mechanisms that underlie the regulation of histone methylation during this repair remain to be further defined. Here, we show that exposure to ionizing radiation induces DNA-PK-dependent phosphorylation of nuclear fumarase at Thr 236, which leads to an interaction between fumarase and the histone variant H2A.Z at DNA double-strand break (DSB) regions. Locally generated fumarate inhibits KDM2B histone demethylase activity, resulting in enhanced dimethylation of histone H3 Lys 36; in turn, this increases the accumulation of the Ku70-containing DNA-PK at DSB regions for non-homologous end-joining DNA repair and cell survival. These findings reveal a feedback mechanism that underlies DNA-PK regulation by chromatin-associated fumarase and an instrumental function of fumarase in regulating histone H3 methylation and DNA repair.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Survival
  • DNA Breaks, Double-Stranded
  • DNA Repair*
  • DNA-Activated Protein Kinase / metabolism
  • F-Box Proteins / metabolism
  • Fumarate Hydratase / metabolism
  • Fumarates / metabolism*
  • HeLa Cells
  • Histones / metabolism*
  • Humans
  • Jumonji Domain-Containing Histone Demethylases / metabolism
  • Methylation
  • Molecular Sequence Data
  • Protein Binding
  • Protein Processing, Post-Translational*
  • Protein Transport

Substances

  • F-Box Proteins
  • Fumarates
  • Histones
  • Jumonji Domain-Containing Histone Demethylases
  • KDM2A protein, human
  • DNA-Activated Protein Kinase
  • Fumarate Hydratase