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Papers In Press, published online ahead of print June 29, 2001
J. Biol. Chem, 10.1074/jbc.M100389200
Submitted on January 16, 2001
Revised on June 18, 2001
Accepted on June 28, 2001

The Delta and Delta' subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation

Min-Sun Song, Phuong T. Pham, Matthew Olson, Jeffrey R. Carter, Mary Ann Franden, Roel M. Schaaper, and Charles S. McHenry

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

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

Delta and delta' are required for assembly of the processivity factor beta onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. We developed protocols for generating highly purified preparations of delta and delta'. In holoenzyme reconstitution assays, delta' could not be replaced by delta, tau or gamma, even when either of the latter were present at a 10,000-fold molar excess. Likewise, delta could not be replaced by delta', tau or gamma. Bacterial strains bearing chromosomal knockouts of either the holA(delta) or holB (delta') genes were not viable, demonstrating that both delta and delta' are essential. Western blots of isolated initiation complexes demonstrated the presence of both delta and delta'. However, in the absence of chi-psi and SSB, a stable initiation-complex lacking delta-delta' was isolated by gel filtration. Lack of delta-delta' decreased the rate of elongation about 3-fold and the extent of processive replication was significantly decreased. Adding back delta-delta', but not chi-psi, delta or delta' alone restored the diminished activity, indicating that in addition to being key components required for the beta loading-activity of the DnaX-complex, delta-delta' are present in initiation-complex and are required for processive elongation.


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