Error-Prone DNA Polymerases
Open accessAbstract
Studies on several recently discovered error-prone DNA polymerases reveal novel structures that may explain the low fidelity of this general class of enzymes, a number of which are involved in the replicative bypass (translesion synthesis) of base damage in DNA.
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Crystal structures reveal that polymerase binding to DNA strongly reshapes the primer-template, for example the backbone at the templating base can be bent by 90°.
“Crystal structures (Refs.15-22 and references therein) reveal that polymerase binding to DNA strongly reshapes the primertemplate, e.g. the backbone at the templating base can be bent by 90°.”
From DNA Replication Fidelity (2004) · cites this paper as [20]
These ideas are supported by structural information and by a report that the insertion fidelity of yeast Pol η is severely impaired with difluorotoluene, a nonpolar isosteric analog of thymine that is unable to form Watson-Crick hydrogen bonds with adenine.
“These ideas are supported by structural information (20, 21, 26 -28) and by a report (29) that the insertion fidelity of yeast Pol is severely impaired with difluorotoluene, a nonpolar isosteric analog of thymine that is unable to form Watson-Crick hydrogen bonds with adenine.”
From DNA Replication Fidelity (2004) · cites this paper as [20]
Certain Y family polymerases are suggested to be in a closed conformation without dNTP, yet kinetic data have emphasized the importance of a dNTP-induced conformational change preceding chemistry to the fidelity of Pol η.
“Moreover, certain Y family polymerases are suggested to be in a closed conformation without dNTP (Refs.20 and 21 but also see comments in Ref. 28), yet kinetic data (40) have emphasized the importance of a dNTP-induced conformational change preceding chemistry to the fidelity of Pol .”
From DNA Replication Fidelity (2004) · cites this paper as [20]
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Mouse models of DNA polymerases
Menezes, M. R., & Sweasy, J. B. (2012) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21731 · Cited by 9 · see citing works
Arana, M. E., Song, L., Gac, N. T. L., Parris, D. S., Villani, G., & Boehmer, P. E. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.02.006 · Cited by 9 · see citing works
Lupus autoantibodies to native DNA preferentially bind DNA presented on PolIV
Kumar, S., Bunting, K. A., Kalsi, J., Hinks, J. A., Latchman, D. S., Pearl, L. H., & Isenberg, D. A. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02090.x · Cited by 7 · see citing works
Sommer, S., Bécherel, O. J., Coste, G., Bailone, A., & Fuchs, R. P. (2003) · DNA repair · doi:10.1016/j.dnarep.2003.08.008 · Cited by 7 · see citing works
Facing Stalled Replication Forks: The Intricacies of Doing the Right Thing
Rudolph, C. J., Schürer, K. A., & Kramer, W. (2006) · Springer eBooks · doi:10.1007/7050_003 · Cited by 7 · see citing works
Liu, L., Sun, D., & Liu, H. (2025) · Molecular Biology and Evolution · doi:10.1093/molbev/msaf252 · Cited by 5 · see citing works
Mechanisms for High Fidelity DNA Replication
McElhinny, S. A. N., Pursell, Z. F., & Kunkel, T. A. (2009) · Royal Society of Chemistry eBooks · doi:10.1039/9781847559852-00086 · Cited by 5 · see citing works
Effect of pH on the Misincorporation Rate of DNA Polymerase η
Nishimoto, N., Suzuki, M., & Izuta, S. (2016) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00900 · Cited by 4 · see citing works
Structures of human telomerase with BIBR1532 reveal novel mechanism of inhibition
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Self-citationFriedberg, E. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.x114.572115 · Cited by 3 · see citing works
Self-citation
- Authors
- Friedberg, E. C., Fischhaber, P. L., & Kisker, C.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- State University of New York (US)
- Corresponding author
- Friedberg, Errol C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 107
- Issue
- 1
- Pages
- 9-12
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1966195927
- Cited by
- 130
- References
- 16
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 3 · 2012: 5
- FWCI
- 6.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- error-prone DNA polymerases, DNA polymerase fidelity, translesion synthesis, DNA damage, polymerase structure, DNA replication
- MeSH terms
- Amino Acid Sequence, DNA Damage, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Protein Conformation, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray
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