The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport

Science. 2017 Feb 24;355(6327):eaag1789. doi: 10.1126/science.aag1789.

Abstract

DNA charge transport chemistry offers a means of long-range, rapid redox signaling. We demonstrate that the [4Fe4S] cluster in human DNA primase can make use of this chemistry to coordinate the first steps of DNA synthesis. Using DNA electrochemistry, we found that a change in oxidation state of the [4Fe4S] cluster acts as a switch for DNA binding. Single-atom mutations that inhibit this charge transfer hinder primase initiation without affecting primase structure or polymerization. Generating a single base mismatch in the growing primer duplex, which attenuates DNA charge transport, inhibits primer truncation. Thus, redox signaling by [4Fe4S] clusters using DNA charge transport regulates primase binding to DNA and illustrates chemistry that may efficiently drive substrate handoff between polymerases during DNA replication.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • DNA / biosynthesis
  • DNA / metabolism*
  • DNA Primase / chemistry*
  • DNA Primase / genetics
  • DNA Replication
  • Electrolysis
  • Humans
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / genetics
  • Mutation
  • Oxidation-Reduction
  • Polymerization
  • Protein Binding
  • Protein Domains

Substances

  • Iron-Sulfur Proteins
  • DNA
  • DNA Primase