Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".

O'Brien E, Holt ME, Thompson MK, Salay LE, Ehlinger AC, Chazin WJ, Barton JK
Science. 2017 357 (6348)

PMID: 28729485 · PMCID: PMC5935490 · DOI:10.1126/science.aan2762

Baranovskiy and Pellegrini argue that, based on structural data, the path for charge transfer through the [4Fe4S] domain of primase is not feasible. Our manuscript presents electrochemical data directly showing charge transport through DNA to the [4Fe4S] cluster of a primase p58C construct and a reversible switch in the DNA-bound signal with oxidation/reduction, which is inhibited by mutation of three tyrosine residues. Although the dispositions of tyrosines differ in different constructs, all are within range for microsecond electron transfer.

Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.

MeSH Terms (6)

Biological Transport DNA DNA Primase Electron Transport Humans Oxidation-Reduction

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