6m3t

Publication Abstract from PubMed

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 approximately 1.96 A 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.

Crystal structure of the mouse endonuclease G.,Park KH, Yoon SM, Song HN, Yang JH, Ryu SE, Woo EJ Biochem Biophys Res Commun. 2020 May 21;526(1):35-40. doi:, 10.1016/j.bbrc.2020.03.060. Epub 2020 Mar 16. PMID:32192768^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.