The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport-Reference-Cited by-同舟云学术

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

Published:2017-02-24 Issue:6327 Volume:355 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

O’Brien Elizabeth¹^ORCID,Holt Marilyn E.²^ORCID,Thompson Matthew K.²,Salay Lauren E.²^ORCID,Ehlinger Aaron C.²^ORCID,Chazin Walter J.²^ORCID,Barton Jacqueline K.¹^ORCID

Affiliation:

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

2. Departments of Biochemistry and Chemistry, Center for Structural Biology, Vanderbilt University, Nashville, TN 37235, USA.

Abstract

DNA charged with regulating replication DNA can transport electrical charge over long distances and has the potential to act as a signaling system. The iron-sulfur complex [4Fe4S] found in some proteins is known to be involved in redox reactions. The eukaryotic DNA primase is involved in DNA replication and contains a [4Fe4S] cluster that is required for its RNA primer synthesis activity. O'Brien et al. show that the [4Fe4S] cluster in DNA primase can regulate the protein's DNA binding activity through DNA-mediated charge transfer. This in turn plays a role in primer initiation and length determination. Science , this issue p. eaag1789

Funder

National Institutes of Health

Gordon and Betty Moore Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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5. Multiplexed Electrochemistry of DNA-Bound Metalloproteins

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