Article
Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair.
Nature communications - 9 Dec 2014
Sone Kenbun, Piao Lianhua, Nakakido Makoto, Ueda Koji, Jenuwein Thomas, Nakamura Yusuke, Hamamoto Ryuji
Abstract excerpt
The presence of phosphorylated histone H2AX (γ-H2AX) is associated with the local activation of DNA-damage repair pathways. Although γ-H2AX deregulation in cancer has previously been reported, the molecular mechanism involved and its relationship with other histone modifications remain largely unknown. Here we find that the histone methyltransferase SUV39H2 methylates histone H2AX on lysine 134. When H2AX was...
Topics
- Animals
- COS Cells
- Cell Separation
- Chlorocebus aethiops
- Chromatin
- DNA Breaks, Double-Stranded
- DNA Damage
- DNA Repair
- Fibroblasts
- Flow Cytometry
- Gamma Rays