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Annual Review of Biochemistry

Volume 88, 2019

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

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]3+ cluster versus the reduced [4Fe4S]2+ 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.

Keyword(s): base excision repair, DNA charge transport, DNA polymerase, DNA primase, iron–sulfur clusters, oxidative stress, redox signaling
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/content/journals/10.1146/annurev-biochem-013118-110644
2019-06-20
2024-04-25
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/content/journals/10.1146/annurev-biochem-013118-110644
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Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication
Annual Review of Biochemistry 88, 163 (2019); https://doi.org/10.1146/annurev-biochem-013118-110644
/content/journals/10.1146/annurev-biochem-013118-110644
/content/journals/10.1146/annurev-biochem-013118-110644
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