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Vol. 11, No. 23,
pp. 3122-3127,
December 1, 1997
1 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724 USA; 2 Graduate Program in Genetics, State University of New York, Stony Brook, New York 11794 USA
Upon infection of human cells, the herpes simplex virus protein
VP16 associates with the endogenous cell-proliferation factor HCF. VP16
can also associate with HCFs from invertebrates, suggesting that VP16
mimics a cellular protein whose interaction with HCF has been
conserved. Here, we show that VP16 mimics the human basic leucine-zipper protein LZIP, which, through association with HCF, may
control cell-cycle progression. VP16 and LZIP share a tetrapeptide motif
D/EHXY
used to associate with
human HCF. The LZIP-related Drosophila protein
BBF-2/dCREB-A contains this HCF-binding motif, indicating that the LZIP-HCF interaction has been conserved during metazoan evolution.
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