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Vol. 11, No. 23, pp. 3122-3127, December 1, 1997

RESEARCH COMMUNICATION
Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP

Richard N. Freiman,1,2 and Winship Herr1,3

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.


GENES & DEVELOPMENT 11:3122-3127 © 1997 by Cold Spring Harbor Laboratory Press ISSN 0890-9369/97 $5.00

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