Partial purification and characterization of mitochondrial DNA polymerase from Plasmodium falciparum

2000 ◽  
Vol 49 (4) ◽  
pp. 279-288 ◽  
Author(s):  
Porntip Chavalitshewinkoon-Petmitr ◽  
Srisucha Chawprom ◽  
Lieve Naesens ◽  
Jan Balzarini ◽  
Prapon Wilairat
FEBS Letters ◽  
1997 ◽  
Vol 410 (2-3) ◽  
pp. 509-514 ◽  
Author(s):  
Melissa A White ◽  
J.Clinton Bailey II ◽  
Gordon C Cannon ◽  
Sabine Heinhorst

1994 ◽  
Vol 41 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S Sen ◽  
S Mukhopadhyay ◽  
J Wetzel ◽  
T K Biswas

The mitochondrial DNA (mtDNA) polymerase was isolated from a protease-deficient yeast strain (PY2), and purified about 3000 fold by a column chromatography on phosphocellulose, heparin-agarose, and single-stranded DNA cellulose. The purified polymerase was characterized with respect to optimal nucleotide concentrations, template-primer specificity and sensitivity to some inhibitors. These results were compared with the nuclear DNA polymerase I activity. Both polymerases showed similar requirement of deoxynucleotide concentrations (Km < 1 microM), and highest activity with poly(dA-dT) template. However, the mtDNA polymerase was more sensitive to ddTTP, EtBr and Mn2+ inhibition in comparison to the nuclear DNA polymerase I. The mtDNA polymerase did not need ATP as an energy source for in vitro DNA synthesis. This mtDNA polymerase preparation also showed 3'-->5' exonuclease activity.


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