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Originally published In Press as doi:10.1074/jbc.M009828200 on November 14, 2000

J. Biol. Chem., Vol. 276, Issue 6, 4433-4440, February 9, 2001
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tau Binds and Organizes Escherichia coli Replication Proteins through Distinct Domains
PARTIAL PROTEOLYSIS OF TERMINALLY TAGGED tau  TO DETERMINE CANDIDATE DOMAINS AND TO ASSIGN DOMAIN V AS THE alpha  BINDING DOMAIN*

Dexiang Gao and Charles S. McHenry

From the Department of Biochemistry and Molecular Genetics and Program in Molecular Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262

The tau  subunit dimerizes Escherichia coli DNA polymerase III core through interactions with the alpha  subunit. In addition to playing critical roles in the structural organization of the holoenzyme, tau  mediates intersubunit communications required for efficient replication fork function. We identified potential structural domains of this multifunctional subunit by limited proteolysis of C-terminal biotin-tagged tau  proteins. The cleavage sites of each of eight different proteases were found to be clustered within four regions of the tau  subunit. The second susceptible region corresponds to the hinge between domain II and III of the highly homologous delta ' subunit, and the third region is near the C-terminal end of the tau -delta ' alignment (Guenther, B., Onrust, R., Sali, A., O'Donnell, M., and Kuriyan, J. (1997) Cell 91, 335-345). We propose a five-domain structure for the tau  protein. Domains I and II are based on the crystallographic structure of delta ' by Guenther and colleagues. Domains III-V are based on our protease cleavage results. Using this information, we expressed biotin-tagged tau  proteins lacking specific protease-resistant domains and analyzed their binding to the alpha  subunit by surface plasmon resonance. Results from these studies indicated that the alpha  binding site of tau  lies within its C-terminal 147 residues (domain V).

* This work was supported by Grant GM35695 from the National Institutes of Health.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.

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


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