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Originally published In Press as doi:10.1074/jbc.M104956200 on August 14, 2001

J. Biol. Chem., Vol. 276, Issue 42, 39340-39349, October 19, 2001
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Building a Replisome Solution Structure by Elucidation of Protein-Protein Interactions in the Bacteriophage T4 DNA Polymerase Holoenzyme*,

Stephen C. AlleyDagger §, Michael A. TrakselisDagger , M. Uljana MayerDagger , Faoud T. IshmaelDagger , A. Daniel JonesDagger , and Stephen J. BenkovicDagger ||

From the Dagger  Department of Chemistry, the Pennsylvania State University and  Department of Biochemistry and Molecular Biology, Hershey Medical Center, the Pennsylvania State University, University Park, Pennsylvania 16802

Assembly of DNA replication systems requires the coordinated actions of many proteins. The multiprotein complexes formed as intermediates on the pathway to the final DNA polymerase holoenzyme have been shown to have distinct structures relative to the ground-state structures of the individual proteins. By using a variety of solution-phase techniques, we have elucidated additional information about the solution structure of the bacteriophage T4 holoenzyme. Photocross-linking and mass spectrometry were used to demonstrate interactions between I107C of the sliding clamp and the DNA polymerase. Fluorescence resonance energy transfer, analytical ultracentrifugation, and isothermal titration calorimetry measurements were used to demonstrate that the C terminus of the DNA polymerase can interact at two distinct locations on the sliding clamp. Both of these binding modes may be used during holoenzyme assembly, but only one of these binding modes is found in the final holoenzyme. Present and previous solution interaction data were used to build a model of the holoenzyme that is consistent with these data.

* This work was supported by National Institutes of Heath Grants GM13306 (to S. J. B.), GM19492 (to S. C. A.), and DK19691 (to F. T. I.), and a fellowship from the Jane Coffin Childs Memorial Fund for Medical Research (to M. U. M).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.

The on-line version of this article (available at http://www.jbc.org) contains a movie of the Fig. 7 model in motion.

§ Current address: Chiron Corp., 201 Elliott Ave. West, Suite 150, Seattle, WA 98119.

|| To whom correspondence should be addressed: Dept. of Chemistry, 414 Wartik Laboratory, the Pennsylvania State University, University Park, PA 16802. Tel.: 814-865-2882; Fax: 814-865-2973; E-mail: sjb1@psu.edu.

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


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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.