pubmed-article:9463369 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9463369 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:9463369 | lifeskim:mentions | umls-concept:C0079405 | lld:lifeskim |
pubmed-article:9463369 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:9463369 | lifeskim:mentions | umls-concept:C0887839 | lld:lifeskim |
pubmed-article:9463369 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:9463369 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:9463369 | pubmed:dateCreated | 1998-3-26 | lld:pubmed |
pubmed-article:9463369 | pubmed:abstractText | Replication of human immunodeficiency virus type 1 (HIV-1) in non-dividing cells critically depends on import of the viral pre-integration complex into the nucleus. Genetic evidence suggests that viral protein R (Vpr) and matrix antigen (MA) are directly involved in the import process. An in vitro assay that reconstitutes nuclear import of HIV-1 pre-integration complexes in digitonin-permeabilized cells was used to demonstrate that Vpr is the key regulator of the viral nuclear import process. Mutant HIV-1 pre-integration complexes that lack Vpr failed to be imported in vitro, whereas mutants that lack a functional MA nuclear localization sequence (NLS) were only partially defective. Strikingly, the import defect of the Vpr- mutant was rescued when recombinant Vpr was re-added. In addition, import of Vpr- virus was rescued by adding the cytosol of HeLa cells, where HIV-1 replication had been shown to be Vpr-independent. In a solution binding assay, Vpr associated with karyopherin alpha, a cellular receptor for NLSs. This association increased the affinity of karyopherin alpha for basic-type NLSs, including that of MA, thus explaining the positive effect of Vpr on nuclear import of the HIV-1 pre-integration complex and BSA-NLS conjugates. These results identify the biochemical mechanism of Vpr function in transport of the viral pre-integration complex to, and across, the nuclear membrane. | lld:pubmed |
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pubmed-article:9463369 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9463369 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9463369 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9463369 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9463369 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9463369 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:PopovSS | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:BlobelGG | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:LeeM AMA | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:RatnerLL | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:MooreM SMS | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:LaneC MCM | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:BukrinskyMM | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:RexachMM | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:ZybarthGG | lld:pubmed |
pubmed-article:9463369 | pubmed:author | pubmed-author:ReilingNN | lld:pubmed |
pubmed-article:9463369 | pubmed:issnType | Print | lld:pubmed |