The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.
Open accessAbstract
A quantitative assay based on gel electrophoresis is described to measure nucleotide insertion kinetics at an arbitrary DNA template site. The assay is used to investigate kinetic mechanisms governing the fidelity of DNA synthesis using highly purified Drosophila DNA polymerase alpha holoenzyme complex and M13 primer-template DNA. Km and Vmax values are reported for correct insertion of A and misinsertion of G, C, and T opposite a single template T site. The misinsertion frequencies are 2 X 10(-4) for G-T and 5 X 10(-5) for both C-T and T-T relative to normal A-T base pairs. The dissociation constant of the polymerase-DNA-dNTP complex, as measured by Km, plays a dominant role in determining the rates of forming right and wrong base pairs. Compared with Km for insertion of A opposite T (3.7 +/- 0.7 microM), the Km value is 1100-fold greater for misinsertion of G opposite T (4.2 +/- 0.4 mM), and 2600-fold greater for misinsertion of either C or T opposite T (9.8 +/- 4.2 mM). These Km differences indicate that in the enzyme binding site the stability of A-T base pairs is 4.3 kcal/mol greater than G-T pairs and 4.9 kcal/mol greater than C-T or T-T pairs. In contrast to the large differences in Km, differences in Vmax are relatively small. There is only a 4-fold reduction in Vmax for insertion of G opposite T and an 8-fold reduction for C or T opposite T, compared with the correct insertion of A. For the specific template T site investigated, the nucleotide insertion fidelity for Drosophila polymerase alpha seems to be governed primarily by a Km discrimination mechanism.
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Citations
Cites
Enzyme structure and mechanism
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Nucleotide sequence of the filamentous bacteriophage M13 DNA genome: comparison with phage fd
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Nucleotide insertion kinetics opposite abasic lesions in DNA.
Randall, S. K., Eritja, R., Kaplan, B. E., Petruska, J. A., & Goodman, M. F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48324-x · Cited by 209
Self-citationScheuermann, R. H., Tam, S., Burgers, P., Lu, C., & Echols, H. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.23.7085 · Cited by 209
The mutational specificity of DNA polymerases-alpha and -gamma during in vitro DNA synthesis.
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Self-citationPetruska, J. A., Sowers, L. C., & Goodman, M. F. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.6.1559 · Cited by 150
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Fidelity of HIV-1 reverse transcriptase
Preston, B. D., Poiesz, B. J., & Loeb, L. A. (1988) · Science · doi:10.1126/science.2460924 · Cited by 931
Biochemical Basis of DNA Replication Fidelity
Goodman, M. F., Creighton, S., Bloom, L. B., Petruska, J., & Kunkel, T. A. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309086792 · Cited by 446
Self-citationComparison between DNA melting thermodynamics and DNA polymerase fidelity.
Petruska, J., Goodman, M. F., Boosalis, M. S., Sowers, L. C., Cheong, C., & Tinoco, I. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6252 · Cited by 316
Self-citationpolι, a remarkably error-prone human DNA polymerase
Tissier, A., McDonald, J. P., Frank, E. G., & Woodgate, R. (2000) · Genes & Development · doi:10.1101/gad.14.13.1642 · Cited by 315
Longley, M. J., Nguyen, D., Kunkel, T. A., & Copeland, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105230200 · Cited by 270
Metadata
- Authors
- Boosalis, M. S., Petruska, J., & Goodman, M. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-10
- Volume
- 262
- Issue
- 30
- Pages
- 14689-14696
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1597138031
- Cited by
- 332
- References
- 23
- FWCI
- 3.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Boosalis, M. S., Petruska, J., & Goodman, M. F. (1987). DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)47850-7
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