Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP.
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.
Pubmed ID: 9389645 RIS Download
Amino Acid Sequence | Animals | Binding Sites | Cell Division | Cell Line, Transformed | Cyclic AMP Response Element-Binding Protein A | DNA-Binding Proteins | Drosophila Proteins | Drosophila melanogaster | HeLa Cells | Herpes Simplex Virus Protein Vmw65 | Herpesvirus 1, Human | Host Cell Factor C1 | Humans | Leucine Zippers | Mice | Molecular Mimicry | Molecular Sequence Data | Proteins | Recombinant Fusion Proteins | Sequence Homology, Amino Acid | Transcription Factors