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

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

Author information

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.

PMID:
28729484
PMCID:
PMC5741086
DOI:
10.1126/science.aan2396
[Indexed for MEDLINE]
Free PMC Article

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