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Papers In Press, published online ahead of print July 17, 2002
J. Biol. Chem, 10.1074/jbc.M202897200
Submitted on March 25, 2002
Revised on July 16, 2002
Accepted on July 16, 2002
Program of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021
Corresponding Author: j-hurwitz{at}ski.mskcc.org
Schizosaccharomyces pombe (sp) DNA polymerase (Pol) 
contains four subunits, Pol 3, Cdc1, Cdc27 and Cdm1. In this report, we examined the role of Cdc27 on the structure and activity of Pol . We show that the four-subunit complex is monomeric in structure, in contrast to the previous report that it was a dimer (Zuo, S., Bermudez, V., Zhang, G., Kelman, Z. and Hurwitz, J. (2000) J. Biol. Chem. 275, 5153-5162). The discrepancy between the earlier and recent observations was traced to the marked asymmetric shape of Cdc27. Cdc27 contains two critical domains that govern its role in activating Pol . The N-terminal region (aa 1-160) binds to Cdc1 and its extreme C-terminal end (aa 362-369) interacts with PCNA. Mutants of spPol, containing truncated Cdc27 derivatives deficient in binding to PCNA, supported DNA replication less processively than the wild-type complex. Fusion of a minimal PCNA binding motif (aa 352-372 to C-terminally truncated Cdc27 derivatives, restored processive DNA synthesis in vitro. In vivo, the introduction of these fused Cdc27 derivatives into cdc27? cells, conferred viability. These data support the model in which Cdc27 plays an essential role in DNA replication by recruiting PCNA to the Pol holoenzyme.
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