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

Andrey G Baranovskiy; Nigar D Babayeva; Yinbo Zhang; Luis Blanco; Youri I Pavlov; Tahir H Tahirov

doi:10.1126/science.aan2396

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

Science. 2017 Jul 21;357(6348):eaan2396. doi: 10.1126/science.aan2396.

Authors

Andrey G Baranovskiy¹, Nigar D Babayeva¹, Yinbo Zhang², Luis Blanco³, Youri I Pavlov^{1

4

5}, Tahir H Tahirov⁶

Affiliations

¹ Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.
² Department of Immunology, University of Washington, Seattle WA 98195, USA.
³ Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid 28049, Spain.
⁴ Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198, USA.
⁵ Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA.
⁶ Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA. ttahirov@unmc.edu.

Abstract

O'Brien et al (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Biological Transport
DNA
DNA Primase / genetics*
Humans
Iron-Sulfur Proteins / genetics
Oxidation-Reduction*

Substances

Iron-Sulfur Proteins
DNA
DNA Primase

Grants and funding

R01 GM101167/GM/NIGMS NIH HHS/United States