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Originally published In Press as doi:10.1074/jbc.M204754200 on June 26, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33041-33048, September 6, 2002
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Protein Determinants of RNA Binding by DNA Polymerase of the T4-related Bacteriophage RB69*

Vasiliy M. PetrovDagger , San-san Ng§, and Jim D. KaramDagger

From the Dagger  Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112

DNA polymerase (gp43) of phage T4 plays two biological roles, one as an essential DNA binding replication enzyme and the other as an mRNA-specific autogenous translational repressor. Binding of T4 gp43 to its mRNA target (translational operator RNA) interferes with gp43-DNA interactions, but it is unclear how the protein determinants for binding DNA are affected by the dynamics of gp43-mRNA interactions. We have used RB69 gp43, a natural variant of the T4 enzyme whose crystal structure has been determined to identify protein sites that respond to the interaction with specific RNA. We used protein phosphorylation markers, photocross-linking studies, protease sensitivity assays, and mutational analyses to examine the effects of operator RNA on the enzyme's five structural domains (N, exo, palm, fingers, and thumb). Our studies suggest that this RNA affects gp43-DNA interactions through global effects on protein structure that occlude DNA-binding sites but leave the enzyme accessible to interactions with the sliding clamp (RB69 gp45) and possibly other polymerase accessory proteins. We discuss the possible biological significance of putative RNA-binding motifs in the N and palm domains of RB69 gp43.

* This work was supported by NIGMS, National Institutes of Health, Grant 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.

§ Present address: Dept. of Genetics, Louisiana State University Health Sciences Center, 533 Bolivar St., New Orleans, LA 70112.

To whom correspondence should be addressed: Dept. of Biochemistry SL 43, Tulane University Health Sciences Center, 1430 Tulane Ave., New Orleans, LA. Tel.: 504-584-1995; Fax: 504-584-1611; E-mail: karamoff@tulane.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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