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Originally published In Press as doi:10.1074/jbc.M002376200 on June 30, 2000

J. Biol. Chem., Vol. 275, Issue 37, 28816-28825, September 15, 2000
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Subunit Interactions within the Saccharomyces cerevisiae DNA Polymerase epsilon  (pol epsilon ) Complex
DEMONSTRATION OF A DIMERIC pol epsilon *

Rajiv Dua, Shaune Edwards, Daniel L. Levy, and Judith L. CampbellDagger

From the Braun Laboratories, California Institute of Technology, Pasadena, California 91125

Saccharomyces cerevisiae DNA polymerase epsilon (pol epsilon ) is essential for chromosomal replication. A major form of pol epsilon  purified from yeast consists of at least four subunits: Pol2p, Dpb2p, Dpb3p, and Dpb4p. We have investigated the protein/protein interactions between these polypeptides by using expression of individual subunits in baculovirus-infected Sf9 insect cells and by using the yeast two-hybrid assay. The essential subunits, Pol2p and Dpb2p, interact directly in the absence of the other two subunits, and the C-terminal half of POL2, the only essential portion of Pol2p, is sufficient for interaction with Dpb2p. Dpb3p and Dpb4p, non-essential subunits, also interact directly with each other in the absence of the other two subunits. We propose that Pol2p·Dpb2p and Dpb3p·Dpb4p complexes interact with each other and document several interactions between individual members of the two respective complexes. We present biochemical evidence to support the proposal that pol epsilon  may be dimeric in vivo. Gel filtration of the Pol2p·Dpb2p complexes reveals a novel heterotetrameric form, consisting of two heterodimers of Pol2p·Dpb2p. Dpb2p, but not Pol2p, exists as a homodimer, and thus the Pol2p dimerization may be mediated by Dpb2p. The pol2-E and pol2-F mutations that cause replication defects in vivo weaken the interaction between Pol2p and Dpb2p and also reduce dimerization of Pol2p. This suggests, but does not prove, that dimerization may also occur in vivo and be essential for DNA replication.

* This work was supported by United States Public Health Service Grant 25508 and Grant 1153-F12 from the American Heart Association (to R. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Braun Laboratories 147-75, California Institute of Technology, Pasadena, CA 91125. Tel.: 626-395-6053; Fax: 626-405-9452; E-mail: jcampbel@cco.caltech.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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