358 0

Crystal structure of the mouse endonuclease G

Title
Crystal structure of the mouse endonuclease G
Author
류성언
Keywords
Apoptosis; Crystal structure; EndoG; Endonuclease; EndoG inhibitors
Issue Date
2020-03
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v. 526, NO 1, Page. 35-40
Abstract
Endonuclease G (EndoG) is a mitochondrial enzyme that responds to apoptotic stimuli by translocating to the nucleus and cleaving the chromatin DNA. The molecular mechanism of EndoG still remains unknown in higher organisms. Here, we determined the crystal structure of mouse EndoG at similar to 1.96 angstrom resolution. The EndoG shows an altered dimeric configuration in which N-terminal region of one subunit interact to the other subunit in dimer. The deletion of this region that is highly conserved in mammalian EndoGs resulted in a monomer with significantly reduced activity suggesting the association of the dimeric arrangement into the nuclease activity. Furthermore, we observed a large conformational change in the loop of the active site groove in EndoG, which corresponds to the DNA binding region. Intriguingly, EndoG dimers are linked by oxidation of the reactive cysteine 110 in this flexible loop to form a long oligomeric chain in the crystal lattice. The structural analysis and ensuing biochemical data suggest that this flexible loop region in the active site is important to the regulation of EndoG nuclease function in mouse. (C) 2020 Elsevier Inc. All rights reserved.
URI
https://www.sciencedirect.com/science/article/pii/S0006291X20305453?via%3Dihubhttps://repository.hanyang.ac.kr/handle/20.500.11754/162650
ISSN
0006-291X; 1090-2104
DOI
10.1016/j.bbrc.2020.03.060
Appears in Collections:
COLLEGE OF ENGINEERING[S](공과대학) > BIOENGINEERING(생명공학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE