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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1994-6-30
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pubmed:abstractText |
vpr is an accessory gene of human immunodeficiency virus I (HIV-I). Although unnecessary for viral replication in T cell lines, growing evidence suggests that it is essential for virus replication in monocytes/macrophages and for replication in vivo. We expressed HIV-I vpr in Escherichia coli and purified Vpr by affinity chromatography. In a coprecipitation assay, the purified Vpr interacted specifically with a cellular protein designated as Vpr-interacting protein, or RIP. Mutational analysis suggested that this interaction required a domain rich in leucine/isoleucine residues and highly conserved between HIV-I and SIVmac Vprs. During transient expression in mammalian cells, HIV-I Vpr was localized in the nucleus. However, mutational analysis failed to identify in Vpr a typical nuclear localization signal rich in basic amino acid residues. Instead, Vpr nuclear localization seemed to correlate with Vpr interaction with RIP. Mutations in the C-terminal 20-amino acid region containing a cryptic nuclear localization signal did not abolish Vpr nuclear localization or interaction with RIP, whereas point mutations in the leucine/isoleucine-rich domain abolished Vpr interaction with RIP and rendered Vpr unstable during transient expression. These results suggest that RIP may be involved in Vpr function.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
269
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pubmed:geneSymbol |
vpr
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15577-82
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8195203-Amino Acid Sequence,
pubmed-meshheading:8195203-Animals,
pubmed-meshheading:8195203-Base Sequence,
pubmed-meshheading:8195203-Binding Sites,
pubmed-meshheading:8195203-Carrier Proteins,
pubmed-meshheading:8195203-Cell Line,
pubmed-meshheading:8195203-Cell Nucleus,
pubmed-meshheading:8195203-Cloning, Molecular,
pubmed-meshheading:8195203-DNA Primers,
pubmed-meshheading:8195203-Escherichia coli,
pubmed-meshheading:8195203-Gene Products, vpr,
pubmed-meshheading:8195203-Genes, vpr,
pubmed-meshheading:8195203-Genome, Viral,
pubmed-meshheading:8195203-HIV-1,
pubmed-meshheading:8195203-HeLa Cells,
pubmed-meshheading:8195203-Humans,
pubmed-meshheading:8195203-Molecular Sequence Data,
pubmed-meshheading:8195203-Mutagenesis, Site-Directed,
pubmed-meshheading:8195203-Oligonucleotides, Antisense,
pubmed-meshheading:8195203-Polymerase Chain Reaction,
pubmed-meshheading:8195203-Recombinant Proteins,
pubmed-meshheading:8195203-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8195203-Restriction Mapping,
pubmed-meshheading:8195203-Sequence Homology, Amino Acid,
pubmed-meshheading:8195203-Transfection,
pubmed-meshheading:8195203-vpr Gene Products, Human Immunodeficiency Virus
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pubmed:year |
1994
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pubmed:articleTitle |
Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein.
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pubmed:affiliation |
Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City 66160-7424.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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