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Papers In Press, published online ahead of print October 17, 2001
J. Biol. Chem, 10.1074/jbc.M107936200
Submitted on August 17, 2001
Revised on October 12, 2001
Accepted on October 16, 2001

Carboxyl-terminal domain III of the Delta' subunit of DNA polymerase III holoenzyme binds DnaX and supports cooperative DnaX-complex assembly

Min-Sun Song and Charles S. McHenry

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

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

The delta' subunit of the DNA polymerase-III holoenzyme is a key component of the DnaX complex; it is required for loading the beta processivity factor onto a primed template. The X-ray crystal structure of delta' indicates a three domain C-shaped structure (Guenther, B., Onrust, R., Sali, A., O'Donnell, M., and Kuriyan, J. (1997) Cell 91, 335-345). In this study, we localized the DnaX-binding domain of delta' to its carboxyl-terminal domain III by quantifying protein-protein interactions using a series of delta' fusion-proteins lacking specific domains. The fusion protein corresponding to domain III of delta' bound to DnaX with an affinity approaching that of full-length delta'. In contrast, a construct bearing delta' domains I-II did not bind DnaX at detectable levels. The presence of delta and chi-psi strengthened the interaction of DnaX with full-length delta' and delta' domain III. Thus, domain III of delta' not only contains the DnaX binding site, but also contains the elements required for positive cooperative assembly of the DnaX complex. A domain III-specific anti-delta' monoclonal antibody interfered with DnaX complex formation and abolished the replication activity of DNA polymerase III holoenzyme.


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