Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication.

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ID: 43019
2019
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Abstract
Many DNA-processing enzymes have been shown to contain a [4Fe4S] cluster, a common redox cofactor in biology. Using DNA electrochemistry, we find that binding of the DNA polyanion promotes a negative shift in [4Fe4S] cluster potential, which corresponds thermodynamically to a ∼500-fold increase in DNA-binding affinity for the oxidized [4Fe4S] cluster versus the reduced [4Fe4S] cluster. This redox switch can be activated from a distance using DNA charge transport (DNA CT) chemistry. DNA-processing proteins containing the [4Fe4S] cluster are enumerated, with possible roles for the redox switch highlighted. A model is described where repair proteins may signal one another using DNA-mediated charge transport as a first step in their search for lesions. The redox switch in eukaryotic DNA primases appears to regulate polymerase handoff, and in DNA polymerase δ, the redox switch provides a means to modulate replication in response to oxidative stress. We thus describe redox signaling interactions of DNA-processing [4Fe4S] enzymes, as well as the most interesting potential players to consider in delineating new DNA-mediated redox signaling networks.
Reference Key
barton2019redoxannual Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Barton, Jacqueline K;Silva, Rebekah M B;O'Brien, Elizabeth;
Journal Annual Review of Biochemistry
Year 2019
DOI
10.1146/annurev-biochem-013118-110644
URL
Keywords
oxidative stress dna charge transport dna polymerase dna primase base excision repair iron–sulfur clusters redox signaling

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