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J. Biol. Chem., Vol. 276, Issue 37, 35217-35222, September 14, 2001

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Assembly of DNA Polymerase III Holoenzyme
CO-ASSEMBLY OF  AND  IS INHIBITED BY DnaX COMPLEX ACCESSORY PROTEINS BUT STIMULATED BY DNA POLYMERASE III CORE^*

Arthur E. Pritchard and Charles S. McHenry

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

Although the two alternative Escherichia coli dnaX gene products,  and , 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 nine-subunit assembly containing  but not . We developed a new assay based on the binding of complexes containing biotin-tagged  to streptavidin-coated agarose beads to investigate the effects of various DNA polymerase III holoenzyme subunits on the kinetics of co-assembly of  and  into the same complex. Auxiliary proteins in combination with ' almost completely blocked co-assembly, whereas or ' alone slowed the association only moderately compared with the interaction of  with  alone. In contrast, DNA polymerase III core, in the absence of ' and , accelerated the co-assembly of  and , suggesting a role for DNA polymerase III' [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]