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

Journal: Science (New York, N.Y.) 2017;357(6348):eaan2396

PMID: 28729484

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Abstract

O'Brien (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.

Address: Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.; Department of Immunology, University of Washington, Seattle WA 98195, USA.; Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid 28049, Spain.; Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198, USA.; Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA.; Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA. [email protected].

DOI: 10.1126/science.aan2396

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MeSH Terms: Biological Transport, DNA, DNA Primase, Humans, Iron-Sulfur Proteins, Oxidation-Reduction