T7 DNA polymerase

T7 DNA polymerase

The T7 DNA polymerase of the T7 bacteriophage is a DNA-dependent DNA polymerase responsible for the fast rate of T7 phage DNA replication "in vivo". The polymerase consists of a 1:1 complex of the viral T7 gene 5 protein (80kDA) and the E. coli thioredoxin (12kDA).

It lacks a 5' -> 3' exonuclease domain, but the 3' -> 5' exonuclease activities are approximately 1000-fold greater than that of Klenow fragment. [cite journal |author=Sambrook, J., Russell, D.W. |title=Molecular Cloning: A Laboratory Manual, Third edition |journal=Cold Spring Harbor Laboratory Press |location=Cold Spring Harbor, New York, 2001. |year=2001 ] The exonuclease activity appears to be responsible for the high fidelity of this enzyme and prevents strand displacement synthesis [cite journal |author=LECHNER, R. L. AND RICHARDSON, C. C. |journal=J. Biol. Chem. |title=A preformed, topologically stable replication fork. |volume= 258 |year=1983 |pages= 11185-11196] This polymerase is unique due to its considerable processivity, or ability to stay on DNA for a greater than average number of base pairs. This makes it particularly useful for recombinant protein expression systems; Using the T7 promoter and T7 polymerase strongly drive the inserted gene of interest without inducing host protein overexpression. It is also suitable for site-directed mutagenesis [cite journal |author=BEBENEK, K. et al. |journal=Nucl. Acids Res. |title=The use of native T7 DNA polymerase for site-directed mutagenesis. |volume= 17 |year=1989 |pages= 5408] but is not recommended for DNA sequencing applications.

[cite journal |author=Doublie S., Tabor S., Long A., Richardson C., and Ellenberger T. |journal=Nature |title=Crystal Structure of a Bacteriophage T7 DNA Replication complex at 2.2 A Resolution. |volume= 391 |year=1998 |pages=251-258]

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