SUBFUNCTIONALIZATION OF ENDONUCLEASE G ISOZYMES IN XENOPUS TROPICALIS

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Endonuclease G (EndoG) is known to be involved in apoptotic degradation of nuclear DNA. It has also been proposed to carry out mRNA degradation in the cytoplasm of apoptotic cells. In the present work, predictive bioinformatics analysis and comparative homology modeling were used to reveal subfunctionalization of two EndoG isozymes (xtEndoG) in the Xenopus tropicalis western clawed frog. The analysis suggests that mitochondrial translocation of one of these proteins can be regulated by calcium-dependent phosphorylation in the region of its N-terminal signal sequence. Detailed comparison of modeled 3D structures of the two proteins reveals thermodynamic and structural differences that affect local protein stability. Our findings bring to light a novel mechanism that can possibly regulate mitochondrial translocation of EndoG and provide a rationale for the existence of two highly homologous xtEndoG proteins in Xenopus tropicalis. Here, we also discuss a probable involvement of the calcium-dependent mechanism of EndoG translocation in frog egg apoptosis.

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