Figure 5

Effect of exonuclease activity on polymerase activity of saPolX. Primer extension assays were performed on a recessed (R) and gapped DNA (dG) substrates to check the role of exonuclease activity on restricting the nucleotide insertion by polymerase domain of saPolX. The enzymatic activities were checked on both the DNA substrates with wt-saPolX and H435A mutant. The results show that H435A exo- mutant inserts higher number of nucleotides on both the substrates as compared to the wt-saPolX. The exonuclease activity residing in the PHP domain of saPolX limits the incorporation of nucleotides by the polymerization activity of the polymerase domain.