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Protein Engineering, Vol. 13, No. 1, 41-47, January 2000
© 2000 Oxford University Press

Functional interdependence of DNA polymerizing and 3'->5' exonucleolytic activities in Pyrococcus furiosus DNA polymerase I

Kayoko Komori and Yoshizumi Ishino1

Department of Molecular Biology, Biomolecular Engineering Research Institute (BERI), 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan

Pyrococcus furiosus DNA polymerase I (Pol BI) belongs to the family B ({alpha}-like) DNA polymerases and has a strong 3'->5' exonucleolytic activity, in addition to its DNA polymerizing activity. To understand the relationship between the structure and function of this DNA polymerase, three deletion mutants, {Delta}1 ({Delta}Leu746–Ser775), {Delta}2 ({Delta}Leu717–Ser775) and {Delta}3 ({Delta}His672–Ser775), and two substituted mutants of Asp405, D405A and D405E, were constructed. These substitutions affected both the DNA polymerizing and the 3'->5' exonucleolytic activities. The {Delta}1 mutant protein had DNA polymerizing activity with higher specific activity than that of the wild-type Pol BI, but retained only 10% of the exonucleolytic activity of the wild-type. The other two deletion mutants lost most of both activities. These results suggest that the DNA polymerizing and exonucleolytic activities are closely related to each other in the folded structure of this DNA polymerase, as proposed in the family B DNA polymerases.


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