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

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

Published:2017-07-21 Issue:6348 Volume:357 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Baranovskiy Andrey G.¹^ORCID,Babayeva Nigar D.¹,Zhang Yinbo²^ORCID,Blanco Luis³^ORCID,Pavlov Youri I.¹⁴⁵,Tahirov Tahir H.¹^ORCID

Affiliation:

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.

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.

Funder

National Institute of General Medical Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference14 articles.

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

2. Crystal structure of the C-terminal domain of human DNA primase large subunit

3. Crystal Structure of the Human Primase

4. Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome

5. Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase

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