Most of the studies devoted to the analysis of the cell death process
in Leishmania indicate that the parasite quickly degrades its DNA. The analysis of the Leishmania genome does not reveal the existence of a nuclease similar to mammalian caspase-activated DNase (CAD), the nuclease mainly involvedinDNAdegradation during apoptosis in mammals. In addition to CAD, mammalian cells possess a second nuclease activity, endonuclease G (EndoG), a mitochondrial nuclease that translocates to the nucleus during apoptosis to degrade chromatinDNAinto nucleosomal fragments in several caspase-independent cell death models. This nuclease
is encoded in a nuclear gene and it is transported to the mitochondria
where it serves diverse functions related to replication, repair and degradation of mitochondrial DNA (mtDNA). EndoG belongs to the -metal superfamily of DNA/RNA non-specific nucleases, requires Mg2+ or other divalent cations for activity, and it is inhibited by moderate salt concentrations (100–150mMNaCl).
Now,I want to know, which domain of endonuclease G (EndoG) cause of apoptosis and which domain of this enzyme cause of proliferation in leishmania infantum? I need to sequence of these domains.
Dear Dr. Azami,
comparison with the human ortholog of EndoG might help to answer one part (apoptosis) of your question:
Varecha M et al. Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis. Mol.Cell. Biochem. 2012; 363: 301 (Figure 4).
The authors of this paper might have more detailed information about interacting sequences..
Best regards,
ML
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