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Objective: To characterize the molecular and biochemical features of the Endonuclease G of Leishmania (Viannia) panamensis.
Methods: The gene of the putative L. (V.) panamensis Endonuclease G was amplified, cloned, and sequenced. The recombinant protein was produced in a heterologous expression system and biochemical assays were run to determine its ion, temperature, and pH preferences.
Results: The L. (V.) panamensis rENDOG has biochemical features similar to those found in other trypanosomatids and higher eukaryotes. In addition, phylogenetic analysis revealed a possible evolutionary relationship with metazoan ENDOG.
Conclusions: L. (V.) panamensis has a gene that codifies an ENDOG homologous to those of higher organisms. This enzyme can be produced in Escherichia coli and is able to degrade covalently closed circular double-stranded DNA. It has a magnesium preference, can be inhibited by potassium, and is able to function within a wide temperature and pH range.
Toro-Londoño, M. A., Patiño, E. B., Robledo, S. M., Jiménez-Ruiz, A., & Alzate, J. F. (2011). Leishmania (Viannia) panamensis expresses a nuclease with molecular and biochemical features similar to the Endonuclease G of higher eukaryotes*. Colombia Medica, 42(2), 154–165.


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Received 2011-06-13
Accepted 2011-06-13