Cited by 700DNA Repair MechanismsDNA and Nucleic Acid ChemistryGenomics and Chromatin Dynamics

Eukaryotic DNA Polymerases

Hübscher, Ulrich, Maga, Giovanni, Spadari, Silvio·2002·Annual Review of Biochemistry

Abstract

▪ Abstract Any living cell is faced with the fundamental task of keeping the genome intact in order to develop in an organized manner, to function in a complex environment, to divide at the right time, and to die when it is appropriate. To achieve this goal, an efficient machinery is required to maintain the genetic information encoded in DNA during cell division, DNA repair, DNA recombination, and the bypassing of damage in DNA. DNA polymerases (pols) α, β, γ, δ, and ϵ are the key enzymes required to maintain the integrity of the genome under all these circumstances. In the last few years the number of known pols, including terminal transferase and telomerase, has increased to at least 19. A particular pol might have more than one functional task in a cell and a particular DNA synthetic event may require more than one pol, which suggests that nature has provided various safety mechanisms. This multi-functional feature is especially valid for the variety of novel pols identified in the last three years. These are the lesion-replicating enzymes pol ζ, pol η, pol ι, pol κ, and Rev1, and a group of pols called pol θ, pol λ, pol μ, pol σ, and pol φ that fulfill a variety of other tasks.

Integrity signals

Registry

Crossref · 10.1146/annurev.biochem.71.090501.150041

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164 of 164 references verified0 citation errors · 0 not checkable

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  • Cells harbor multiple DNA polymerases, many of which have only been discovered in the past 5 years and whose cellular functions are not fully understood.

    “To perform these tasks, cells harbor multiple DNA polymerases (2,3), many of which have only been discovered in the past 5 years and whose cellular functions are not fully understood.”

    From DNA Replication Fidelity (2004) · cites this paper as [2]

  • Although many template-dependent human polymerases lack intrinsic proofreading activity, it is possible that dissociation from DNA after misinsertion may allow proofreading by the exonuclease activity intrinsic to another replication or repair protein, such as Pol δ, Pol ε, or apurinic/apyrimidinic endonuclease.

    “Although many (e.g. at least 10 of 15 template-dependent human) polymerases lack intrinsic proofreading activity (2, 3), it is possible that dissociation from DNA after misinsertion may allow proofreading by the exonuclease activity intrinsic to another replication or repair protein, such as Pol ␦, Pol ⑀, or apurinic/apyrimidinic endonuclease (50).”

    From DNA Replication Fidelity (2004) · cites this paper as [2]

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Authors
Hübscher, U., Maga, G., & Spadari, S.
Affiliations
University of Zurich (CH)
Venue
Annual Review of Biochemistry
Published
2002-06
Volume
71
Issue
1
Pages
133-163
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2163221081
Cited by
691
References
164
Citations by year
2026: 6 · 2025: 4 · 2024: 6 · 2023: 7 · 2022: 5 · 2021: 15 · 2020: 18 · 2019: 15 · 2018: 10 · 2017: 16 · 2016: 20 · 2015: 16 · 2014: 25 · 2013: 41 · 2012: 47
FWCI
4.10
Type
journal article
Language
en
Open access
closed
Locations
  • Annual Review of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
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 › Genomics and Chromatin Dynamics
Keywords
eukaryotic DNA polymerases, genome stability, DNA replication, DNA repair, DNA recombination, DNA damage bypass, Pol eta, Rev1, telomerase, terminal transferase
MeSH terms
Animals, Binding Sites, DNA, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, DNA-Binding Proteins, Humans, Models, Molecular, Recombination, Genetic, Protein Structure, Tertiary, Proliferating Cell Nuclear Antigen, Telomerase, Protein Subunits, Replication Protein C

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