The human checkpoint sensor Rad9–Rad1–Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase

Guan, Xin; Madabushi, Amrita; Chang, Dau-Yin; Fitzgerald, Megan E.; Shi, Gouli; Drohat, Alexander C.; Lu, A-Lien

doi:10.1093/nar/gkm678

Cited by 65DNA Repair MechanismsDNA and Nucleic Acid ChemistryEpigenetics and DNA Methylation

The human checkpoint sensor Rad9–Rad1–Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase

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Guan, Xin, Madabushi, Amrita, Chang, Dau-Yin, Fitzgerald, Megan E., Shi, Gouli, Drohat, Alexander C., Lu, A-Lien·2007·Nucleic Acids Research

DOI 10.1093/nar/gkm678PMC PMC2094074

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Abstract

Human (h) DNA repair enzyme thymine DNA glycosylase (hTDG) is a key DNA glycosylase in the base excision repair (BER) pathway that repairs deaminated cytosines and 5-methyl-cytosines. The cell cycle checkpoint protein Rad9-Rad1-Hus1 (the 9-1-1 complex) is the surveillance machinery involved in the preservation of genome stability. In this study, we show that hTDG interacts with hRad9, hRad1 and hHus1 as individual proteins and as a complex. The hHus1 interacting domain is mapped to residues 67-110 of hTDG, and Val74 of hTDG plays an important role in the TDG-Hus1 interaction. In contrast to the core domain of hTDG (residues 110-308), hTDG(67-308) removes U and T from U/G and T/G mispairs, respectively, with similar rates as native hTDG. Human TDG activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. Interestingly, the interaction between hRad9 and hTDG, as detected by co-immunoprecipitation (Co-IP), is enhanced following N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) treatment. A significant fraction of the hTDG nuclear foci co-localize with hRad9 foci in cells treated with methylating agents. Thus, the 9-1-1 complex at the lesion sites serves as both a damage sensor to activate checkpoint control and a component of the BER.

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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 [185]

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Authors: Guan, X., Madabushi, A., Chang, D.-Y., Fitzgerald, M. E., Shi, G., Drohat, A. C., & Lu, A.-L.
Affiliations: University of Maryland, Baltimore (US)
Corresponding author: Lu, A-Lien
ORCID: Guan, Xin
Drohat, Alexander C.
Lu, A-Lien
Venue: Nucleic Acids Research
Publisher: Oxford University Press (OUP)
Published: 2007-09
Volume: 35
Issue: 18
Pages: 6207-6218
ISSN: 0305-1048 (ISSN-L)
1362-4962
DOI: 10.1093/nar/gkm678
PMC: PMC2094074
OpenAlex: W1982176904
Cited by: 65
References: 87
Citations by year: 2026: 1 · 2024: 1 · 2022: 1 · 2021: 1 · 2018: 3 · 2017: 1 · 2016: 3 · 2015: 8 · 2014: 2 · 2013: 12 · 2012: 3
FWCI: 2.91
Type: journal article
Language: en
Open access: gold
doi.org
Locations: Nucleic Acids Research (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc)
PubMed (publishedVersion)
Funders: Universität Basel
National Institutes of Health
University of North Carolina at Chapel Hill
University of California, Irvine
National Cancer Institute (CA78391, R01CA078391, R56CA078391)
National Institute of General Medical Sciences (GM-072711, T32GM066706, R01GM072711, GM066706)
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 › Molecular Biology › Epigenetics and DNA Methylation
Keywords: thymine DNA glycosylase, base excision repair, DNA glycosylase activity, protein-protein interaction, DNA mismatch repair, MNNG, methylating agents, genome stability, DNA damage recognition, cytosine deamination, 5-methylcytosine
MeSH terms: Amino Acid Sequence, Binding Sites, DNA Damage, DNA Repair, Enzyme Activation, Exonucleases, HeLa Cells, Humans, Molecular Sequence Data, Cell Cycle Proteins, Thymine DNA Glycosylase

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The human checkpoint sensor Rad9–Rad1–Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase

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