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Journal:Cell reports

Abstract:Endonuclease G (EndoG) is a mitochondrial protein that is released from mitochondria and relocated into the nucleus to promote chromosomal DNA fragmentation during apoptosis. Here, we show that oxidative stress causes cell-death defects in C. elegans through an EndoG-mediated cell-death pathway. In response to high reactive oxygen species (ROS) levels, homodimeric CPS-6-the C. elegans homolog of EndoG-is dissociated into monomers with diminished nuclease activity. Conversely, the nuclease activity of CPS-6 is enhanced, and its dimeric structure is stabilized by its interaction with the worm AIF homolog, WAH-1, which shifts to disulfide cross-linked dimers under high ROS levels. CPS-6 thus acts as a ROS sensor to regulate the life and death of cells. Modulation of the EndoG dimer conformation could present an avenue for prevention and treatment of diseases resulting from oxidative stress.

All the Authors:Riley Skeen-Gaar,Wei-Zen Yang,Pei Zhao,Zhe Zhang,Xiao Ge,Shohei Mitani

First Author:Jason LJ Lin#,Akihisa Nakagawa#

Indexed by:Journal paper

Correspondence Author:Ding Xue*,Hanna S Yuan*

Document Code:8

Translation or Not:no

Date of Publication:2016-07-01

Included Journals:SCI