Yeast DNA Polymerase η Utilizes an Induced-Fit Mechanism of Nucleotide Incorporation
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DNA polymerase eta (Poleta) is unique among eukaryotic DNA polymerases in its proficient ability to replicate through distorting DNA lesions, and Poleta synthesizes DNA with a low fidelity. Here, we use pre-steady-state kinetics to investigate the mechanism of nucleotide incorporation by Poleta and show that it utilizes an induced-fit mechanism to selectively incorporate the correct nucleotide. Poleta discriminates poorly between the correct and incorrect nucleotide at both the initial nucleotide binding step and at the subsequent induced-fit conformational change step, which precedes the chemical step of phosphodiester bond formation. This property enables Poleta to bypass lesions with distorted DNA geometries, and it bestows upon the enzyme a low fidelity.
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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 [40]
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References 54 · Cited by 123
Research works printed but not linked: 1
- Zhou, B.-L., Pata, J.D., and Steitz, T.A. (2001). Crystal structure of Proc. Natl. Acad. Sci. USA 92, 719-723.
- Authors
- Washington, M. T., Prakash, L., & Prakash, S.
- Affiliations
- The University of Texas Medical Branch at Galveston (US)
- Corresponding author
- Prakash, Satya
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-12
- Volume
- 107
- Issue
- 7
- Pages
- 917-927
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2114243500
- Cited by
- 123
- References
- 54
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 7 · 2015: 6 · 2014: 6 · 2013: 4
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm019261-30)
- National Institute of General Medical Sciences (GM-19261)
- 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 › Protein Structure and Dynamics
- Keywords
- DNA polymerase eta, induced fit, nucleotide incorporation, nucleotide discrimination, pre-steady-state kinetics, DNA damage bypass, conformational change, phosphodiester bond formation, nucleotide binding
- MeSH terms
- Y-Family DNA Polymerases, DNA, DNA-Directed DNA Polymerase, DNA Repair, Kinetics, Nucleotides, Saccharomyces cerevisiae, Substrate Specificity
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