Interaction of Checkpoint Proteins Hus1/Rad1/Rad9 with DNA Base Excision Repair Enzyme MutY Homolog in Fission Yeast, Schizosaccharomyces pombe
Open accessAbstract
The DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated opposite DNA strands containing guanine or 7,8-dihydro-8-oxoguanine by base excision repair thereby preventing G:C to T:A mutations. MYH has been shown to interact with the proliferating cell nuclear antigen (PCNA) in both human and fission yeast Schizosaccharomyces pombe systems. Here we show that S. pombe (Sp) MYH physically interacts with all subunits of the PCNA-like checkpoint protein heterotrimer, SpRad9/SpRad1/SpHus1, in yeast extracts and when the individual subunits are expressed in bacteria. The SpHus1 and SpPCNA binding sites are located in discrete regions of SpMYH. Immunoprecipitation assays reveal that the interaction between SpHus1 and SpMYH increases dramatically after hydrogen peroxide treatment, and this increase in the SpHus1-SpMYH interaction correlates with the presence of SpHus1 phosphorylation. In contrast, the interaction between SpPCNA and SpMYH after hydrogen peroxide treatment remains nearly unchanged. SpMYH associates with SpHus1 in a complex of approximately 450 kDa, the reported native molecular mass of the SpRad9/SpRad1/SpHus1-MYC complex. A larger portion of SpMYH shifts to the 150-500-kDa regions after hydrogen peroxide treatment in comparison with untreated extracts. SpHus1 phosphorylation is substantially reduced in SpMYH Delta cells after hydrogen peroxide treatment. These data suggest that MYH may act as an adaptor to recruit checkpoint proteins to the DNA lesions.
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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 [179]
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References 61 · Cited by 85
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- Authors
- Chang, D.-Y., & Lu, A.-L.
- Affiliations
- University of Maryland, Baltimore (US)
- Corresponding author
- Lu, A-Lien
- ORCID
- Lu, A-Lien
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-01
- Volume
- 280
- Issue
- 1
- Pages
- 408-417
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2002820477
- Cited by
- 85
- References
- 61
- Citations by year
- 2026: 1 · 2024: 1 · 2022: 1 · 2021: 5 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 3 · 2014: 4 · 2013: 11 · 2012: 4
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Medical Research Council
- National Cancer Institute (CA/ES78391)
- National Institute of General Medical Sciences (R01GM035132, GM 35132)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- MUTYH, base excision repair, DNA glycosylase, DNA damage checkpoint, Hus1, RAD1, Rad9, PCNA, protein-protein interaction, hydrogen peroxide, protein phosphorylation, 8-oxoguanine, Schizosaccharomyces pombe
- MeSH terms
- DNA Repair, DNA-Binding Proteins, Endonucleases, Phosphorylation, Protein Binding, Schizosaccharomyces, Cell Cycle Proteins, Protein Subunits, Schizosaccharomyces pombe Proteins, DNA Glycosylases, Macromolecular Substances
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