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DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
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Yeast require redox switching in DNA primase.

Elizabeth O'Brien1, Lauren E Salay2,3,4, Esther A Epum5

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.

Proceedings of the National Academy of Sciences of the United States of America
|December 14, 2018
PubMed
Summary

Yeast DNA primase uses a [4Fe4S] cluster as a DNA-mediated redox switch for DNA binding. Specific tyrosines are crucial for this redox switch, with mutations impacting primase function and viability.

Keywords:
DNA charge transportDNA replicationiron–sulfur proteins

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Area of Science:

  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic DNA primases utilize a [4Fe4S] cluster in the p58 subunit (p58C) that influences DNA binding affinity.
  • This cluster's role extends beyond catalysis, acting as a DNA-mediated redox switch.

Purpose of the Study:

  • To investigate the function of the [4Fe4S] cluster and associated tyrosines in yeast DNA primase.
  • To elucidate the mechanism of the DNA-mediated redox switch in eukaryotic primase.

Main Methods:

  • Site-directed mutagenesis of key tyrosine residues (Y395, Y397) in yeast p58C.
  • Analysis of [4Fe4S] cluster redox states and integrity.
  • Assessment of primase function and viability in yeast strains with mutated tyrosines.

Main Results:

  • Mutations in tyrosines Y395 and Y397 alter electron transfer chemistry and the redox switch mechanism.
  • Y395 mutations diminish p58C participation in redox switching.
  • Y397 mutations lead to oxidative cluster degradation and are lethal in yeast.
  • A constellation of tyrosines facilitates protein-DNA electron transfer for the redox switch.

Conclusions:

  • The [4Fe4S] cluster in yeast primase functions as a DNA-mediated redox switch governing DNA binding.
  • Specific tyrosine residues are essential for mediating protein-DNA electron transfer and maintaining cluster integrity.
  • The Y397 residue is critical for primase function in vivo, highlighting the importance of this redox switch mechanism.