Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase.

Biochemistry (1988), Volume 27, Page 6008

Abstract:

We have determined the fidelity of in vitro DNA synthesis catalyzed at high temperature by the DNA polymerase from the thermophilic bacterium Thermus aquaticus. Using a DNA substrate that contains a 3'-OH terminal mismatch, we demonstrate that the purified polymerase lacks detectable exonucleolytic proofreading activity. The fidelity of the Taq polymerase was measured by two assays which score errors produced during in vitro DNA synthesis of the lacZ alpha complementation gene in M13mp2 DNA. In both assays, the Taq polymerase produces single-base substitution errors at a rate of 1 for each 9000 nucleotides polymerized. Frameshift errors are also produced, at a frequency of 1/41,000. These results are discussed in relation to the effects of high temperature on fidelity and the use of the Taq DNA polymerase as a reagent for the in vitro amplification of DNA by the polymerase chain reaction.

Polymerases:

Topics:

Fidelity, Exonuclease Activity

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
Taq pol I Tindall KR1988 3-5' Exonuclease (proofreading) No
Taq pol I Tindall KR1988 Frameshift Error Rate 2.44E-05 errors/bp
Taq pol I Tindall KR1988 Nucleotide Substitution Rate 0.000111 errors/bp
Taq pol I Tindall KR1988 Full length or truncated Full length
Klenow fragment Tindall KR1988 3-5' Exonuclease (proofreading) Yes
Klenow fragment Tindall KR1988 Overall Error Rate 0.0044 errors/bp
Klenow fragment Tindall KR1988 Nucleotide Substitution Rate 4E-05 errors/bp
Klenow fragment Tindall KR1988 Full length or truncated Full length
AMV Tindall KR1988 3-5' Exonuclease (proofreading) No

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