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Originally published In Press as doi:10.1074/jbc.M007707200 on December 22, 2000

J. Biol. Chem., Vol. 276, Issue 13, 10387-10397, March 30, 2001
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Interacting Fidelity Defects in the Replicative DNA Polymerase of Bacteriophage RB69*

Anna BebenekDagger §, Holly Kloos DressmanDagger , Geraldine T. CarverDagger , San-san Ng, Vasiliy Petrov, Guangwei Yang||, William H. Konigsberg||, Jim D. Karam, and John W. DrakeDagger **

From the Dagger  Laboratory of Molecular Genetics, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709-2233, the  Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, and the || Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510-3219

The DNA polymerases (gp43s) of the related bacteriophages T4 and RB69 are B family (polymerase alpha  class) enzymes that determine the fidelity of phage DNA replication. A T4 whose gene 43 has been mutationally inactivated can be replicated by a cognate RB69 gp43 encoded by a recombinant plasmid in T4-infected Escherichia coli. We used this phage-plasmid complementation assay to obtain rapid and sensitive measurements of the mutational specificities of mutator derivatives of the RB69 enzyme. RB69 gp43s lacking proofreading function (Exo- enzymes) and/or substituted with alanine, serine, or threonine at the conserved polymerase function residue Tyr567 (PolY567(A/S/T) enzymes) were examined for their effects on the reversion of specific mutations in the T4 rII gene and on forward mutation in the T4 rI gene. The results reveal that Tyr567 is a key determinant of the fidelity of base selection and that the Pol and Exo functions are strongly coupled in this B family enzyme. In vitro assays show that the PolY567A Exo- enzyme generates mispairs more frequently but extends them less efficiently than does a Pol+ Exo- enzyme. Other replicative DNA polymerases may control fidelity by strategies similar to those used by RB69 gp43.

* This work was supported in part by United States Public Health Service Grants DK09070, GM18842, and GM54627.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Permanent address: Institute of Biochemistry and Biophysics, Polish Academy of Science, 02-106 Warsaw, Poland.

** To whom correspondence should be addressed: Laboratory of Molecular Genetics E3-01, National Institute of Environmental Health Sciences, Rm. E-344, 111 South Alexander Dr., Research Triangle Park, NC 27709. E-mail: drake@niehs.nih.gov.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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