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Volume 272, Number 6, Issue of February 7, 1997 pp. 3398-3405
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Oct-1 POU Homeodomain Stabilizes the Adenovirus Preinitiation Complex via a Direct Interaction with the Priming Protein and Is Displaced when the Replication Fork Passes

(Received for publication, September 12, 1996, and in revised form, November 20, 1996)

From the Laboratory for Physiological Chemistry, Utrecht University, Stratenum, P. O. Box 80042, 3508 TA Utrecht, The Netherlands

Initiation of adenovirus DNA replication is strongly enhanced by two cellular transcription factors, NFI and Oct-1, which bind to the auxiliary origin and tether the viral precursor terminal protein-DNA polymerase (pTP·pol) complex to the core origin. NFI acts through a direct contact with the DNA polymerase, but the mode of action of Oct 1 is unknown.

Employing glutathione S-transferase-POU pull-down assays and protein affinity chromatography, we have established that the POU domain contacts pTP rather than pol. The POU homeodomain is responsible for this interaction. The protein-protein contacts lead to increased binding of pTP-pol to the core origin, which is caused by a reduced off-rate. The enhanced formation of a pTP·pol·POU complex on the origin correlates with stimulation of replication.

Using an immobilized replication system, we have studied the kinetics of dissociation of the Oct-1 POU domain during replication. In contrast to NFI, which dissociates very early in initiation, Oct-1 dissociates only when the binding site is rendered single-stranded upon translocation of the replication fork. Our data indicate that NFI and Oct-1 enhance initiation synergistically by touching different targets in the preinitiation complex and dissociate independently after initiation.

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