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Cited by 98DNA Repair MechanismsDNA and Nucleic Acid ChemistryBacterial Genetics and Biotechnology

The human Rad9–Rad1–Hus1 checkpoint complex stimulates flap endonuclease 1

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Wang, Wensheng, Brandt, Patrick, Rossi, Marie L., Lindsey-Boltz, Laura, Podust, Vladimir, Fanning, Ellen, Sancar, Aziz, Bambara, Robert A.·2004·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0407686101PMC PMC534749
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Abstract

The toroidal damage checkpoint complex Rad9–Rad1–Hus1 (9-1-1) has been characterized as a sensor of DNA damage. Flap endonuclease 1 (FEN1) is a structure-specific nuclease involved both in removing initiator RNA from Okazaki fragments and in DNA repair pathways. FEN1 activity is stimulated by proliferating cell nuclear antigen (PCNA), a toroidal sliding clamp that acts as a platform for DNA replication and repair complexes. We show that 9-1-1 also binds and stimulates FEN1. Stimulation is observed on a variety of flap, nick, and gapped substrates simulating repair intermediates. Blocking 9-1-1 entry to the double strands prevents a portion of the stimulation. Like PCNA stimulation, 9-1-1 stimulation cannot circumvent the tracking mechanism by which FEN1 enters the substrate; however, 9-1-1 does not substitute for PCNA in the stimulation of DNA polymerase β. This suggests that 9-1-1 is a damage-specific activator of FEN1.

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  • The 9-1-1 complex interacts with BER proteins APE1, Pol β, FEN1, DNA ligase I, and DNA glycosylases MutY, NEIL1, and TDG, stimulating their DNA repair activities.

    “As a critical component of ATR-Chk1 checkpoint pathway, the 9-1-1 complex interacts with several BER proteins: APE1, Polymerase β (Pol β), FEN1, DNA ligase I, as well as DNA glycosylases MutY, NEIL1, and TDG, thereby stimulating their DNA repair activities [177–185] (Fig. 3).”

    From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [178]

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Authors
Wang, W., Brandt, P., Rossi, M. L., Lindsey-Boltz, L., Podust, V., Fanning, E., Sancar, A., & Bambara, R. A.
Affiliations
  • University of North Carolina at Chapel Hill (US)
  • Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235-1634; and Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2004-11-19
Volume
101
Issue
48
Pages
16762-16767
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0407686101
PMC
PMC534749
OpenAlex
W2083888152
Cited by
98
References
59
Citations by year
2026: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 4 · 2014: 5 · 2013: 9 · 2012: 3
FWCI
3.80
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
  • UNC Libraries
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM 024441, GM322833, GM-52948, R01GM024441, R01GM052948)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
FEN1, proliferating cell nuclear antigen, DNA damage response, DNA repair, Okazaki fragment processing, DNA replication, DNA polymerase beta
MeSH terms
Base Sequence, DNA Damage, DNA-Binding Proteins, Endonucleases, Enzyme Activation, Humans, Hydrolysis, DNA Primers, Cell Cycle Proteins, Schizosaccharomyces pombe Proteins, Flap Endonucleases

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