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Volume 272, Number 30, Issue of July 25, 1997 pp. 18974-18981
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

A Complex Consisting of Human Replication Factor C p40, p37, and p36 Subunits Is a DNA-dependent ATPase and an Intermediate in the Assembly of the Holoenzyme

(Received for publication, January 17, 1997, and in revised form, May 17, 1997)

Jinsong Cai , Emma Gibbs , Frank Uhlmann , Barbara Phillips , Nina Yao § , Michael O'Donnell § and Jerard Hurwitz

From the Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center and § The Rockefeller University, New York, New York 10021

Human replication factor C (hRFC) is a multi-subunit protein complex capable of supporting proliferating cell nuclear antigen (PCNA)-dependent DNA synthesis by DNA polymerases delta  and epsilon . The hRFC complex consists of five different subunits with apparent molecular masses of 140, 40, 38, 37, and 36 kDa. We have previously reported the expression of a three-subunit core complex, consisting of the p40, p37, and p36 subunits following coupled in vitro transcription-translation of the cDNAs encoding these proteins (Uhlmann, F., Cai, J., Flores-Rozas, H., Dean, F. B., Finkelstein, J., O'Donnell, M., and Hurwitz, J. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 6521-6526). Here we describe the isolation of a stable complex composed of the p40, p37, and p36 subunits of hRFC from baculovirus-infected insect cells. The purified p40·p37·p36 complex, like the five-subunit RFC, contained DNA-dependent ATPase activity that was stimulated by PCNA, preferentially bound to primed DNA templates, interacted with PCNA, and was capable of unloading PCNA from singly-nicked circular DNA. In contrast to the five-subunit RFC, the three-subunit core complex did not load PCNA onto DNA. The p40·p37·p36 complex inhibited the elongation of primed DNA templates catalyzed by the DNA polymerase delta  holoenzyme. Incubation of the p40·p37·p36 complex with the hRFC p140 and p38 subunits formed the five-subunit hRFC complex that supported PCNA-dependent DNA synthesis by DNA polymerase delta .


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