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. 1984 Jul 25;12(14):5897–5911. doi: 10.1093/nar/12.14.5897

The effect of the 3',5' thiophosphoryl linkage on the exonuclease activities of T4 polymerase and the Klenow fragment.

A P Gupta, P A Benkovic, S J Benkovic
PMCID: PMC320039  PMID: 6087297

Abstract

The 3'----5' exonuclease activities of T4 DNA polymerase and the Klenow fragment of Polymerase I towards the phosphoryl and thiophosphoryl 3',5' linkage were examined under comparable conditions of idling-turnover, duplex hydrolysis and turnover during polymerization. With the T4 enzyme there is a negligible effect of thiosubstitution on these activities; with the Klenow fragment there is a greater than one hundred-fold reduction in rate with the thiolinkage for the exonuclease but not polymerization activities. This inability to hydrolyze rapidly the thiophosphoryl linkage extends to the hydrolytic activity of Exonuclease III. The quantitation of the exonuclease activities of these three proteins under various conditions should aid in the successful employment of thiophosphoryl nucleoside triphosphates for their incorporation into DNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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