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Translesion DNA Polymerases
Open accessAbstract
Living cells are continually exposed to DNA-damaging agents that threaten their genomic integrity. Although DNA repair processes rapidly target the damaged DNA for repair, some lesions nevertheless persist and block genome duplication by the cell's replicase. To avoid the deleterious consequence of a stalled replication fork, cells use specialized polymerases to traverse the damage. This process, termed "translesion DNA synthesis" (TLS), affords the cell additional time to repair the damage before the replicase returns to complete genome duplication. In many cases, this damage-tolerance mechanism is error-prone, and cell survival is often associated with an increased risk of mutagenesis and carcinogenesis. Despite being tightly regulated by a variety of transcriptional and posttranslational controls, the low-fidelity TLS polymerases also gain access to undamaged DNA where their inaccurate synthesis may actually be beneficial for genetic diversity and evolutionary fitness.
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“Pol η and Pol ζ can bypass T-T CPDs and were shown to play an important role in TLS of UV damage, while REV1 was shown to be required for bypass of a 6-4 TT dimer in vivo.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [125]
In the citing paper
“Damage tolerance is certainly an unusual repair mechanism employed in response to UV radiation. It allows rapid prevention of consequences of the replication fork arrest [125].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [125]
In the citing paper
“Furthermore, it prevents the formation of double strand breaks in response to UV radiation [125,127].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [125]
In the citing paper
“Moreover, TLS polymerases lack the 3′-5′ exonucleases (proofreading) activity further limiting repair accuracy [125,127].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [125]
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A new model for SOS-induced mutagenesis: how RecA protein activates DNA polymerase V
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DNA polymerase II is encoded by the DNA damage-inducible dinA gene of Escherichia coli.
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Self-citationPivotal role of the β-clamp in translesion DNA synthesis and mutagenesis in E. coli cells
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UmuD and RecA Directly Modulate the Mutagenic Potential of the Y Family DNA Polymerase DinB
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Purification and Characterization of polκ, a DNA Polymerase Encoded by the Human DINB1 Gene
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Translesion DNA polymerases remodel the replisome and alter the speed of the replicative helicase
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Self-citationMutation induced by DNA damage: a many protein affair
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Self-citationLessons from 50 years of SOS DNA-damage-induced mutagenesis
Schlacher, K., & Goodman, M. F. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2198 · Cited by 114
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Self-citationStructural Insight into Translesion Synthesis by DNA Pol II
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Neher, S. B., Sauer, R. T., & Baker, T. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235804100 · Cited by 112
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Proofreading-defective DNA polymerase II increases adaptive mutation in Escherichia coli.
Foster, P. L., Gudmundsson, G., Trimarchi, J. M., Cai, H., & Goodman, M. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7951 · Cited by 109
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Enthalpy-Entropy Compensation in DNA Melting Thermodynamics
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Self-citationPurification of a Soluble UmuD′C Complex from Escherichia coli
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Self-citationRecA acts in trans to allow replication of damaged DNA by DNA polymerase V
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Self-citationThe Escherichia coli polB gene, which encodes DNA polymerase II, is regulated by the SOS system
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Structural diversity of the Y-family DNA polymerases
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Mutagenic repair in Escherichia coli
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Self-citationUvm mutants of Escherichia coli K12 deficient in UV mutagenesis
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Identification of a DinB/UmuC homolog in the archeon Sulfolobus solfataricus
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Self-citationThe two-step model of bacterial UV mutagenesis
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Self-citationDNA polymerase θ (POLQ) can extend from mismatches and from bases opposite a (6-4) photoproduct
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Structure of the Human Rev1–DNA–dNTP Ternary Complex
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dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues
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Characterization of the umu-complementing operon from R391
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Self-citationStructural basis of error‐prone replication and stalling at a thymine base by human DNA polymerase ι
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Pirh2 E3 Ubiquitin Ligase Targets DNA Polymerase Eta for 20S Proteasomal Degradation
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Translesion synthesis in Escherichia coli: Lessons from the NarI mutation hot spot
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Quantitation of the inhibition of hfr x F− recombination by the mutagenesis complex UmuD′C
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Pirh2 E3 Ubiquitin Ligase Monoubiquitinates DNA Polymerase Eta To Suppress Translesion DNA Synthesis
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Replication Bypass of Interstrand Cross-link Intermediates by Escherichia coli DNA Polymerase IV
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Structural Insights into the Generation of Single-Base Deletions by the Y Family DNA Polymerase Dbh
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Escherichia coli DNA polymerase II catalyzes chromosomal and episomal DNA synthesis in vivo
Rangarajan, S., Gudmundsson, G., Qiu, Z., Foster, P. L., & Goodman, M. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.3.946 · Cited by 52
Self-citationFrisch, R. L., Su, Y., Thornton, P. C., Gibson, J. L., Rosenberg, S. M., & Hastings, P. J. (2010) · Journal of Bacteriology · doi:10.1128/jb.00570-10 · Cited by 51
McDonald, J. P. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj512 · Cited by 50
Positive and negative signals between interacting cells for establishing neural fate
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Karata, K., Vaisman, A., Goodman, M. F., & Woodgate, R. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.01.012 · Cited by 39
Self-citationFidelity Mechanisms In DNA Replication
Echols, H. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.60.1.477 · Cited by 38
Villani, G., Hübscher, U., Gironis, N., Parkkinen, S., Pospiech, H., Shevelev, I., di Cicco, G., Markkanen, E., Syväoja, J. E., & Gac, N. T. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.246611 · Cited by 30
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Self-citationCrystallization of DNA Polymerase II from Escherichia coli
Anderson, W. F., Prince, D. B., Yu, H. Y., McEntee, K., & Goodman, M. F. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1765 · Cited by 12
Self-citationShtygasheva, A. A., Belousova, E. A., Rechkunova, N. I., Lebedeva, N. A., & Lavrik, O. I. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908110060 · Cited by 9
Research works printed but not linked: 5
- McDonald JP Frank EG Plosky BS Rogozin IB Masutani C Hanaoka F Woodgate R Gearhart PJ 2003 Identification of a nonsense mutation in DNA polymerase ι from 129-derived strains of mice and its effect on somatic hypermutation J Exp Med 198 635 643 12925679 PMC2194173
- Ogi T Shinkai Y Tanaka K Ohmori H 2002 Polk protects mammalian cells against the lethal and mutagenic effects of polycyclic hydrocarbons Proc Natl Acad Sci 99 15548 15553 12432099 PMC137754
- Pham P Bertram JG O’Donnell M Woodgate R Goodman MF 2001 A model for SOS-lesion targeted mutations in E. coli involving pol V, RecA, SSB and β sliding clamp Nature 409 366 370 11201748
- Qiu Z Goodman MF 1997 The Escherichia coli polB locus is identical to dinA, the structural gene for DNA polymerase II. Characterization of Pol II purified from a polB mutant J Biol Chem 272 8611 8617 9079692
- Trincao J Johnson RE Escalante CR Prakash S Prakash L Aggarwal AK 2001 Structure of the catalytic core of S. cerevisiae DNA polymerase η. Implications for translesion DNA synthesis Mol Cell 8 417 426 11545743
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Metadata
- Authors
- Goodman, M. F., & Woodgate, R.
- Affiliations
- University of Southern California (US)
- National Institutes of Health (US)
- ORCID
- Woodgate, R.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-07-09
- Volume
- 5
- Issue
- 10
- Pages
- a010363-a010363
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3783050
- OpenAlex
- W1971658781
- Cited by
- 317
- References
- 163
- Citations by year
- 2026: 35 · 2025: 19 · 2024: 14 · 2023: 16 · 2022: 30 · 2021: 26 · 2020: 31 · 2019: 22 · 2018: 25 · 2017: 32 · 2016: 22 · 2015: 28 · 2014: 11 · 2013: 6
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM21422, ES012259)
- National Institute of General Medical Sciences (GM 21422, R37GM021422, R01GM021422)
- National Institute of Environmental Health Sciences (ES012259, R01ES012259)
- National Institute of Child Health and Human Development
- Eunice Kennedy Shriver National Institute of Child Health and Human Development
- 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
- translesion synthesis, DNA polymerase, DNA damage tolerance, replication fork stalling, whole-genome duplication, mutagenesis, carcinogenesis, post-translational regulation, transcriptional regulation, DNA repair, genetic diversity
- MeSH terms
- Archaea, DNA Damage, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, Escherichia coli, Humans, Models, Genetic, Saccharomyces cerevisiae, Mutagenesis
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