Hits:

Title of Paper:Oxidative stress impairs cell death by repressing the nuclease activity of mitochondrial endonuclease G

Journal:Cell reports

Summary: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.

First Author:Akihisa Nakagawa#,Jason LJ Lin#

Correspondence Author:Ding Xue*,Hanna S Yuan*

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

Indexed by:Journal paper

Document Code:8

Impact Factor:8.12

DOI Number:10.1016/j.celrep.2016.05.090.

Translation or Not:No

Date of Publication:2016-07

Included Journals:SCI

Release Time:2016-07-01