A Redox Role for the [4Fe4S] Cluster of Yeast DNA Polymerase δ.

ABSTRACT: A [4Fe4S]²⁺ cluster in the C-terminal domain of the catalytic subunit of the eukaryotic B-family DNA polymerases is essential for the formation of active multi-subunit complexes. Here we use a combination of electrochemical and biochemical methods to assess the redox activity of the [4Fe4S]²⁺ cluster in Saccharomyces cerevisiae polymerase (Pol) δ, the lagging strand DNA polymerase. We find that Pol δ bound to DNA is indeed redox-active at physiological potentials, generating a DNA-mediated signal electrochemically with a midpoint potential of 113 ± 5 mV versus NHE. Moreover, biochemical assays following electrochemical oxidation of Pol δ reveal a significant slowing of DNA synthesis that can be fully reversed by reduction of the oxidized form. A similar result is appa

SUBMITTER: Bartels PL 

PROVIDER: S-EPMC5881389 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature