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A more recent version of this article appeared on September 7, 2001
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M102735200v1
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Papers In Press, published online ahead of print July 19, 2001
J. Biol. Chem, 10.1074/jbc.M102735200
Submitted on March 27, 2001
Revised on June 21, 2001
Accepted on July 19, 2001

Assembly of DNA polymerase III holoenzyme co-assembly of gamma and tau is inhibited by DnaX complex accessory proteins but stimulated by DNA polymerase III core

Arthur E. Pritchard and Charles S. McHenry

Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262

Corresponding Author: charles.mchenry{at}uchsc.edu

Although the two alternative Escherichia coli dnaX gene products, tau and gamma , are found co-assembled in purified DNA polymerase III holoenzyme, the pathway of assembly is not well understood. When the 10-subunits of holoenzyme are simultaneously mixed, they rapidly form a 9-subunit assembly containing tau but not gamma . We developed a new assay, based on the binding of complexes containing biotin-tagged tau to streptavidin-coated agarose beads, to investigate the effects of various DNA polymerase III holoenzyme subunits on the kinetics of co-assembly of gamma and tau into the same complex. Auxiliary proteins in combination with delta ' almost completely blocked co-assembly while {chi psi} or delta ' alone slowed the association only moderately compared to the interaction of tau with gamma alone. In contrast, DNA polymerase III core, in the absence of {delta delta}' and {chi psi}, accelerated the co-assembly of tau and gamma , suggesting a role for DNA polymerase III' [tau 2(pol III core)2] in the assembly pathway of holoenzyme.


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B. P. Glover, A. E. Pritchard, and C. S. McHenry
tau Binds and Organizes Escherichia coli Replication Proteins through Distinct Domains. DOMAIN III, SHARED BY gamma AND tau , OLIGOMERIZES DnaX
J. Biol. Chem., September 14, 2001; 276(38): 35842 - 35846.
[Abstract] [Full Text] [PDF]


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