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Cited by 277

The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.

Kinetic mechanism whereby DNA polymerase I (Klenow) replicates DNA with high fidelity

Kuchta, Robert D., Benkovic, Patricia, Benkovic, Stephen J.·1988·Biochemistry
DOI 10.1021/bi00418a012
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Abstract

A complete kinetic scheme describing the polymerization of correct and incorrect dNTPs by the Klenow fragment (KF) of DNA polymerase I has been developed by using short DNA oligomers of defined sequence. The high fidelity arises from a three-stage mechanism. The first stage of discrimination [(1.1 X 10(4-) greater than 1.2 X 10(6]-fold] comes primarily from a dramatically reduced rate of phosphodiester bond formation for incorrect nucleotides, but it also gains a smaller contribution from selective dNTP binding. After phosphodiester bond formation, a conformational change slows dissociation of the incorrect DNA products from KF and, in conjunction with editing by the 3'----5'-exonuclease, increases fidelity 4- greater than 61-fold. Finally, KF polymerizes the next correct dNTP onto a mismatch very slowly, providing a further 6- greater than 340-fold increase in fidelity. Surprisingly, the 3'----5'-exonuclease did not in its hydrolysis reaction differentiate between correctly and incorrectly base-paired nucleotides; rather, an increased lifetime of the enzyme-DNA complex containing the misincorporated base is responsible for discrimination.

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Metadata

Authors
Kuchta, R. D., Benkovic, P., & Benkovic, S. J.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1988-09-06
Volume
27
Issue
18
Pages
6716-6725
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00418a012
OpenAlex
W1969826188
Cited by
277
References
35
FWCI
4.83
Type
journal article
Language
en
Open access
closed

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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