Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP.
Details
Serval ID
serval:BIB_C62D7CA963DE
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP.
Journal
Genes and Development
ISSN
0890-9369[print], 0890-9369[linking]
Publication state
Published
Issued date
1997
Volume
11
Number
23
Pages
3122-3127
Language
english
Notes
Publication types: Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Publication Status: ppublish
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.
Keywords
Amino Acid Sequence, Animals, Binding Sites, Cell Division, Cell Line, Transformed, Cyclic AMP Response Element-Binding Protein A, DNA-Binding Proteins/metabolism, Drosophila Proteins, Drosophila melanogaster, Hela Cells, Herpes Simplex Virus Protein Vmw65/metabolism, Herpesvirus 1, Human/metabolism, Host Cell Factor C1, Humans, Leucine Zippers, Mice, Molecular Mimicry, Molecular Sequence Data, Proteins/genetics, Proteins/metabolism, Recombinant Fusion Proteins/genetics, Recombinant Fusion Proteins/metabolism, Sequence Homology, Amino Acid, Transcription Factors
Pubmed
Web of science
Open Access
Yes
Create date
04/05/2009 12:03
Last modification date
20/08/2019 15:41
Usage data
