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J. Biol. Chem., Vol. 277, Issue 7, 5660-5666, February 15, 2002
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From the Department of Biochemistry and Molecular Biology,
University of Miami School of Medicine, Miami, Florida
33101-6129
Heat shock proteins participate in the initiation
of DNA replication of different organisms by facilitating the assembly
of initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the
viral origins of replication. Hsp40 and Hsp70 act substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this
effect is Hsp40. Heat shock proteins also stimulate the ATPase activity
of UL9 with oriS and increase opening of the origin. In contrast, heat
shock proteins have no effect on the origin-independent activities of
UL9 suggesting that their role is not merely in refolding denatured
protein. These observations are consistent with a role for heat shock
proteins in activating UL9 to efficiently initiate viral
origin-dependent DNA replication. The action of heat shock
proteins in this capacity is analogous to their role in activating the
initiator proteins of other organisms.
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, University of Miami School of Medicine, P.O. Box
016129, Miami, FL 33101-6129. Tel.: 305-243-2934; Fax: 305-243-3955;
E-mail: pboehmer@molbio.med.miami.edu.
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