[7][8] The enzyme encoded by this gene is a member of the conserved DNA/RNA non-specific ββα-Me-finger nuclease family and possesses a unique site selectivity of poly(dG).poly(dC) sequences in double-stranded DNA.

[9][10][11] The H-N-N motif (His-141, Asn-163, Asn-172) is crucial for the protein's catalytic function and substrate specificity, and the His-141 amino acid is necessary for magnesium coordination.

[7][9][11] In one such pathway, caspase-independent apoptosis, the E3 ligase C-terminal of Hsc-70 interacting protein (CHIP), a regulator of EndoG expression, functions as a protective mechanism against oxidative stress.

In later stages of apoptosis the entire cell becomes fragmented, forming a number of plasma membrane-bounded apoptotic bodies which contain nuclear and or cytoplasmic elements.

The ultrastructural appearance of necrosis is quite different, the main features being mitochondrial swelling, plasma membrane breakdown and cellular disintegration.

It has been shown that BNIP3 interacts with the voltage-dependent anion channel (VDAC) to directly induce mitochondrial release and nuclear translocation of EndonucleaseG.

Data has identified VDAC as an interacting partner of BNIP3 and provide direct evidence to support that EndoG is a mediator of the BNIP3 cell death pathway.

Ischemic heart disease, which results from an occlusion of one of the major coronary arteries, is currently still the leading cause of morbidity and mortality in western society.

EndoG has also been implicated in Parkinson's disease (PD), as it induces DNA fragmentation in neurons when translocated from the mitochondria to nuclei.