The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery
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The human checkpoint sensor and alternative clamp Rad9–Rad1–Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9–Rad1–Hus1 with MutY DNA glycosylase, DNA polymerase β and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9–Rad1–Hus1 complex, thus enhancing the quality control of DNA.
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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 [181]
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“Recently, the 9-1-1 complex has been shown to interact with and stimulate the enzymes involved in BER including MYH (35,36), NEIL1 (37), APE1 (38), Polb (39), FEN1 (40,41) and DNA ligase l ( 42 ,43).”
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“DNA ligase 1 also mediates long-patch base excision repair and participates in the 9-1-1 (a checkpoint complex containing Rad9, Hus1 and Rad1) DNA damage response to repair single stranded DNA damage during replicative stress [36,37,38].”
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“Finally, DNA ligase I is the enzyme at the last step of BER, and also associates with as well as is stimulated by the 9-1-1 complex [Smirnova et al., 2005; Wang et al., 2006].”
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“…et al., 2005) as well as base excision repair factors, including the MYH DNA glycosylase , DNA polymerase , flap endonuclease I, and DNA ligase I (Toueille et al., 2004; Wang et al., 2004a. 2006a; Chang and Lu, 2005; Friedrich-Heineken et al., 2005; Smirnova et al., 2005; Shi et al., 2006).”
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“Preparation of DNA substrates The DNA substrate used to measure the ligation activity on a double-stranded substrate carrying a single-strand nick was prepared as described [ 33 ], the 19 nucleotide DNA strand was phosphorylated using γ-[32P]-ATP and T4 polynucleotide kinase (New England Biolabs).”
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“The 9-1-1 may then serve as a scaffold for assembly of DNA repair proteins, Flap endonuclease [38, 39], DNA polymerase β [40], DNA ligase 1 [41], and DNA glycosylase MutY [42], in addition to aiding processing of the DNA ends by its own exonucleolytic activity [43–45].”
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“This latter characteristic is shared not only by many other BER proteins, such as APE1 (30), polymerase b (POLb)(31), FEN1 (32,33), LIG1 (34,35), but also by other DNA glycosylases, such as 8-oxoG DNA glycosylase1 (OGG1) (36), thymine DNA glycosylase (TDG) (37) and endonuclease VIII-like glycosylase1 (NEIL1) (38).”
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“…found to interact with 9A-1-1 include DNA polymerase beta, DNA ligase 1, flap endonuclease 1 (FEN1), MutY human homolog (MYH), apurinic/apyrimidinic endonuclease1 (APE-1) and 8-oxoguanine DNA glycosylase (OGG1) (Smirnova et al. 2005; Gembka et al. 2007; Park et al. 2009; Querol-Audi et al. 2012).”
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“The 9-1-1 complex can also stimulate the FEN1 (Friedrich-Heineken et al., 2005) and DNA ligase I activities (Timson et al., 2000; Smirnova et al., 2005), as observed with PCNA.”
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“excision repair (10, 20, 46, 48, 55, 58, 59) and translesion DNA”
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“Notably, 9-1-1 interacts with, and in many cases stimulates the activity of, multiple factors involved in base excision repair, including flap endonuclease 1 (FEN1),(36) human 8-oxoguanine DNA glycosylase (hOGG1),(37) MutY glycosylase (MYH),(38) DNA polymerase β,(39) and DNA ligase I.(40) Multiple interactions have al…”
BackgroundNeed telomere maintenance? Call 911
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“The checkpoint clamp physically associates with several factors required for base excision repair (BER) [ 5-11 ] and additionally interacts with translesion DNA polymerases [12,13].”
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Blockade of Base Excision Repair
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“…Rad14 nucleotide excision repair protein of S. cerevisiae (Giannattasio et al., 2004), the human FEN1 nuclease (Wang et al., 2004), DNA ligase I (Smirnova et al., 2005), the MYH glycosylase of S. pombe (Chang and Lu, 2005), and the apurinic/apyrimidinic endonuclease 1 (Ape1) of S. cerevisiae…”
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“The 9-1-1 complex also interacts with and stimulates other BER enzymes including APE1 (Gembka et al., 2007), POLbeta (Toueille et al., 2004), FEN1 (Friedrich-Heineken et al., 2005; Wang et al., 2004a), RPA (Wu et al., 2005), and DNA ligase 1 (Smirnova et al., 2005; Wang et al., 2006a).”
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- Authors
- SMIRNOVA, E., TOUEILLE, M., MARKKANEN, E., & HÜBSCHER, U.
- Affiliations
- University of Zurich (CH)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2005-06-21
- Volume
- 389
- Issue
- 1
- Pages
- 13-17
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1184534
- OpenAlex
- W2164443758
- Cited by
- 74
- References
- 32
- Citations by year
- 2026: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2018: 1 · 2015: 4 · 2014: 2 · 2013: 9 · 2012: 2
- FWCI
- 4.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31.61361.00, 61361)
- 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
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- DNA ligase I, long-patch base excision repair, DNA polymerase beta, FEN1, protein-protein interaction
- MeSH terms
- DNA Ligase ATP, DNA Damage, DNA Repair, Enzyme Activation, Exonucleases, Humans, DNA Ligases, Protein Binding, Cell Cycle Proteins, Proliferating Cell Nuclear Antigen, Schizosaccharomyces pombe Proteins, Multiprotein Complexes
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