Human DNA primase is a heterodimeric, DNA-dependent RNA polymerase that initiates replication on single-stranded DNA. Primase has been shown previously to contain a [4Fe4S] cluster cofactor in the C terminal domain of its large subunit (p58C). Here we measure the redox activity of the [4Fe4S] domain of primase (p58C) using electrochemistry on a DNA-modified gold electrode. P58C is found to be electrochemically active on duplex DNA substrates with a single-stranded DNA overhang. Binding of p58C to the DNA substrate, moreover, is found to be dependent both on oxidation state of the [4Fe4S] cluster and on the presence of nucleotide triphosphates (NTPs). Through these studies, we are exploring how DNA charge transport may be exploited by DNA primase in order to execute the multistep, coordinated process of replication initiation.

Investigating the redox properties of human DNA primase

249th National Meeting (2015)

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