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1977•Proceedings of the National Academy of SciencesOpen access

A thermostable sequence-specific endonuclease from Thermus aquaticus.

Showbu Sato, Catherine Hutchinson, J. Ieuan Harris

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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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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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Available 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).

Key concepts: Thermus aquaticus, Thermus, Endonuclease, Thermophile, Cleavage (geology), Bacteriophage, Biology, DNA

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