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Nucleic Acids Research, 1992, Vol. 20, No. 23 6369-6375
© 1992

MOLECULAR BIOLOGY

POU domain transcription factors from different subclasses stimulate adenovirus DNA replication

C.Peter Verrijzer+, Marijke Strating, Yvonne M. Mul and Peter C.van der Vliet*

Laboratory for Physiological Chemistry, University of Utrecht Vondellaan 24a, 3521 GG Utrecht, The Netherlands

*To whom correspondence should be addressed

Received August 4, 1992. Revised October 29, 1992. Accepted October 29, 1992.

POU domain proteins constitute a family of eukaryotic transcription factors that exert critical functions during development. They contain a conserved 160 amino acids DNA binding domain, the POU domain. Genetic data have demonstrated that some POU domain proteins are essential for the proliferation of specific cell types, suggesting a possible role in DNA replication. In addition, the ubiquitous POU transcription factor Oct-1 or its isolated POU domain enhances adenovirus DNA replication. Here we compared the DNA binding specificities of POU domain proteins from different subclasses. They exhibit overlapping, yet distinct binding site preferences. Furthermore, purified Pit-1, Oct-1, Oct-2, Oct-6, Oct-4 and zebrafish POU[C] could all stimulate adenovirus DNA replication in a reconstituted in vitro system. Thus, activation appears to depend on a property common to most POU domain proteins. Adenovirus DNA replication is also stimulated by the transcription factor NFI/CTF. In contrast to NFI, the POU domain did not enhance binding of precursor terminal protein-DNA polymerase to the origin nor did it stabilize the preinitiation complex. These results suggest that the POU domain acts on a rate limiting step after formation of the preinitiation complex.

+ Present address: Department of Molecular and Cell Biology, University of California, Berkeley, USA


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