Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzyme.


Polymerase gamma is solely responsible for fast and faithful replication of the mitochondrial genome. High processivity of the polymerase gamma is often achieved by association of the catalytic subunit with accessory factors that enhance its catalytic activity and/or DNA binding. Here we characterize the intrinsic catalytic activity and processivity of the recombinant catalytic subunit of yeast polymerase gamma, the Mip1 protein. We demonstrate that Mip1 can efficiently synthesize DNA stretches of up to several thousand nucleotides without dissociation from the template. Furthermore, we show that Mip1 can perform DNA synthesis on double-stranded templates utilizing a strand displacement mechanism. Our observations confirm that in contrast to its homologues in other organisms, Mip1 can function as a single-subunit replicative polymerase.



Kinetic Parameters, Source / Purification, Nucleotide Incorporation


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Polymerase Reference Property Result Context
Sce pol gamma Viikov K2011 Processivity 50bp
Sce pol gamma Viikov K2011 Strand Displacement Yes
T7 Viikov K2011 Processivity 257bp
T7 Viikov K2011 Strand Displacement No
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