The Oxidation State of [4Fe4S] Clusters Modulates the DNA-Binding Affinity of DNA Repair Proteins.

ABSTRACT: A central question important to understanding DNA repair is how certain proteins are able to search for, detect, and fix DNA damage on a biologically relevant time scale. A feature of many base excision repair proteins is that they contain [4Fe4S] clusters that may aid their search for lesions. In this paper, we establish the importance of the oxidation state of the redox-active [4Fe4S] cluster in the DNA damage detection process. We utilize DNA-modified electrodes to generate repair proteins with [4Fe4S] clusters in the 2+ and 3+ states by bulk electrolysis under an O₂-free atmosphere. Anaerobic microscale thermophoresis results indicate that proteins carrying [4Fe4S]³⁺ clusters bind to DNA 550 times more tightly than those with [4Fe4S]²⁺ clusters. The mea

SUBMITTER: Tse ECM 

PROVIDER: S-EPMC5929122 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature