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Originally published In Press as doi:10.1074/jbc.M909257199 on March 9, 2000
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J Biol Chem, Vol. 275, Issue 20, 15512-15519, May 19, 2000

Characterization of the Unique C Terminus of the Escherichia coli tau  DnaX Protein
MONOMERIC C-tau BINDS alpha  AND DnaB AND CAN PARTIALLY REPLACE tau  IN RECONSTITUTED REPLICATION FORKS*

H. Garry DallmannDagger §, Sungsub Kim, Arthur E. PritchardDagger , Kenneth J. Marians||, and Charles S. McHenryDagger

From the Dagger  Department of Biochemistry and Molecular Genetics and Molecular Biology Program, University of Colorado Health Sciences Center, Denver, Colorado 80262, the  Graduate Program in Molecular Biology, Cornell University Graduate School of Medical Sciences, New York, New York 10021, and the || Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

A contact between the dimeric tau  subunit within the DNA polymerase III holoenzyme and the DnaB helicase is required for replication fork propagation at physiologically-relevant rates (Kim, S., Dallmann, H. G., McHenry, C. S., and Marians, K. J. (1996) Cell 84, 643-650). In this report, we exploit the OmpT protease to generate C-tau , a protein containing only the unique C-terminal sequences of tau , free of the sequences shared with the alternative gamma  frameshifting product of dnaX. We have established that C-tau is a monomer by sedimentation equilibrium and sedimentation velocity ultracentrifugation. Monomeric C-tau binds the alpha  catalytic subunit of DNA polymerase III with a 1:1 stoichiometry. C-tau also binds DnaB, revealed by a coupled immunoblotting method. C-tau restores the rapid replication rate of inefficient forks reconstituted with only the gamma  dnaX gene product. The acceleration of the DnaB helicase can be observed in the absence of primase, when only leading-strand replication occurs. This indicates that C-tau , bound only to the leading-strand polymerase, can trigger the conformational change necessary for DnaB to assume the fast, physiologically relevant form.

* This work was supported in part by National Institutes of Health Grants GM34557 (to K. J. M.) and GM36255 (to C. S. 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.

§ Supported by a postdoctoral fellowship from the Natural Sciences and Engineering Research Council of Canada. Present address: Tularik Inc., 2 Corporate Dr., South San Francisco, CA 94080.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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