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Nucleic Acids Research, 2003, Vol. 31, No. 16 4702-4709
© 2003 Oxford University Press

Insertion of the T3 DNA polymerase thioredoxin binding domain enhances the processivity and fidelity of Taq DNA polymerase

John F. Davidson, Richard Fox, Dawn D. Harris, Sally Lyons-Abbott and Lawrence A. Loeb*

Department of Pathology, University of Washington, Seattle, WA 98195, USA

*To whom correspondence should be addressed. Tel: +1 206 543 9360; Fax: +1 206 543 3967; Email: laloeb{at}u.washington.edu

Insertion of the T3 DNA polymerase thioredoxin binding domain (TBD) into the distantly related thermostable Taq DNA polymerase at an analogous position in the thumb domain, converts the Taq DNA polymerase from a low processive to a highly processive enzyme. Processivity is dependent on the presence of thioredoxin. The enhancement in processivity is 20–50-fold when compared with the wild-type Taq DNA polymerase or to the recombinant polymerase in the absence of thioredoxin. The recombinant Taq DNA pol/TBD is thermostable, PCR competent and able to copy repetitive deoxynucleotide sequences six to seven times more faithfully than Taq DNA polymerase and makes 2–3-fold fewer AT->GC transition mutations.


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