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

  1. Richard N. Freiman1,2 and
  2. Winship Herr1,3
  1. 1Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724 USA; 2Graduate Program in Genetics, State University of New York, Stony Brook, New York 11794 USA

Abstract

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.

Footnotes

  • 3 Corresponding author.

  • [Key Words: HCF protein; VP16; LZIP; protein–protein interactions; transcription]

  • E-MAIL herr{at}cshl.org; FAX (516) 367-8454.

    • Received August 25, 1997.
    • Accepted September 18, 1997.
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