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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Feb;74(2):542–546. doi: 10.1073/pnas.74.2.542

A thermostable sequence-specific endonuclease from Thermus aquaticus.

S Sato, C A Hutchinson 3rd, J I Harris
PMCID: PMC392326  PMID: 265518

Abstract

A sequence-specific endonuclease, Taq I, of novel specificity has been partially purified from an extreme thermophile, Thermus aquaticus. The enzyme cleaves bacteriophage lambda DNA at many (greater than 30) sites and bacteriophage psiX174 RF DNA at 10 sites. The enzyme is active at temperatures up to 70 degrees. The cleavage sites on psiX174 RF DNA have been mapped. The sequence recognized and cleaved by Taq I has been shown to be the symmetrical tetranucleotide: (formula: see text).

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Selected References

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