Cited by 130DNA Repair MechanismsEnzyme Structure and FunctionProtein Structure and Dynamics

Error-Prone DNA Polymerases

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Friedberg, Errol C., Fischhaber, Paula L., Kisker, Caroline·2001·Cell

Abstract

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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Crossref · 10.1016/s0092-8674(01)00509-8

Cites

16 of 16 references verified0 citation errors · 0 not checkable

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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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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
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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