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

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Eukaryotic DNA Polymerases

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

DOI 10.1146/annurev.biochem.71.090501.150041

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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.

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Quality Control by DNA Repair
Lindahl, T. L., & Wood, R. D. (1999) · Science · doi:10.1126/science.286.5446.1897 · Cited by 1,521
The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists
Alberts, B. (1998) · Cell · doi:10.1016/s0092-8674(00)80922-8 · Cited by 1,411
Telomere states and cell fates
Blackburn, E. H. (2000) · Nature · doi:10.1038/35040500 · Cited by 1,395
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
Masutani, C., Kusumoto, R., Yamada, A., Dohmae, N., Yokoi, M., Yuasa, M., Araki, M., Iwai, S., Takio, K., & Hanaoka, F. (1999) · Nature · doi:10.1038/21447 · Cited by 1,292
DNA Replication Fidelity
Kunkel, T. A., & Bebenek, K. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.497 · Cited by 1,003
Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
Krishna, T. S. R., Kong, X., Gary, S. L., Burgers, P., & Kuriyan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90014-0 · Cited by 902
The Y-Family of DNA Polymerases
Ohmori, H., Friedberg, E. C., Fuchs, R. P., Goodman, M. F., Hanaoka, F., Hinkle, D. C., Kunkel, T. A., Lawrence, C. W., Livneh, Z., Nohmi, T., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00278-7 · Cited by 882
Eukaryotic DNA mismatch repair
Kolodner, R. D., & Marsischky, G. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80013-6 · Cited by 861
DNA Polymerases: Structural Diversity and Common Mechanisms
Steitz, T. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17395 · Cited by 848

Show all 164 references

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10.1046/j.1432-1327.1998.2540209.x · DOI
Hübscher U, Maga G, Podust VN. 1996. InDNA Replication Accessory Proteins, ed. ML De Pamphilis, pp. 525–43. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
10.1016/S1097-2765(00)80361-5 · DOI
Bollum FJ, 1978, Adv. Enzymol., 47, 347

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Authors: Hübscher, U., Maga, G., & Spadari, S.
Affiliations: University of Zurich (CH)
ORCID: Maga, Giovanni
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2002-06
Volume: 71
Issue: 1
Pages: 133-163
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.71.090501.150041
OpenAlex: W2163221081
Semantic Scholar: ac3d6c3b8ed17b4d96d5bade9bc385a4743991c6
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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