CaltechAUTHORS
Published July 20, 2017 | Version Accepted Version
Journal Article Open

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

Creators

  • 1. ROR icon California Institute of Technology
  • 2. ROR icon Vanderbilt University

Abstract

Baranovskiy et al. 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.

Additional Information

© 2017 American Association for the Advancement of Science. 10 April 2017; accepted 13 June 2017.

Attached Files

Accepted Version - nihms947704.pdf

Files

nihms947704.pdf

Files (326.6 kB)

Name Size
md5:22cbfa6357e7cfb854a2c78421aa4c28
326.6 kB Preview Download

Additional details

Identifiers

PMCID
PMC5935490
Eprint ID
79253
DOI
10.1126/science.aan2762
Resolver ID
CaltechAUTHORS:20170720-130038340

Dates

Created
2017-07-20
Created from EPrint's datestamp field
Updated
2022-03-23
Created from EPrint's last_modified field