Hoffmann-la Roche Inc.

Roche Molecular Systems, Inc.

F. Hoffmann-la Roche Ag

Richard D Abramson

David H Gelfand

I Lawrence Greenfield

David H Gelfland

The present invention relates to thermostable DNA polymerases which exhibit a different level of 5' to 3' exonuclease activity than their respective native polymerases. Particular conserved amino acid domains in thermostable DNA polymerases are mutated or deleted to alter the 5' to 3' exonuclease activity of the polymerases. The present invention also relates to means for isolating and producing such altered polymerases.

5' to 3' exonuclease mutations of thermostable DNA polymerases

A purified thermostable enzyme is derived from the eubacterium Thermus species Z05. The enzyme has DNA polymerase, activity reverse transcriptase activity, and optionally 5'.fwdarw.3' exonuclease activity. The enzyme can be native or recombinant, and may be used with primers and nucleoside triphosphates in a temperature-cycling chain reaction where at least one nucleic acid sequence is amplified in quantity from an existing sequence.

DNA encoding thermostable nucleic acid polymerase enzyme from thermus

Mutated thermostable nucleic acid polymerase enzyme from Thermus species

A purified thermostable enzyme is derived from the bacterium Thermus species sps17. The enzyme has DNA polymerase activity, reverse transcriptase activity, and optionally, 5'.fwdarw.3' exonuclease activity. The enzyme can be native or recombinant, and can be used with selected primers and nucleoside triphosphates in a temperature-cycling chain reaction where at least one nucleic acid sequence is amplified in quantity from an existing sequence.

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Oakland, CA, United States of America

Richard D Abramson