Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70
Autor: | Andrew C. S. Saphire, Larry Gerace, Tinglu Guan, Eric C. Schirmer, Glen R. Nemerow |
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Rok vydání: | 2000 |
Předmět: |
Nuclear Envelope
viruses Nuclear Localization Signals Fluorescent Antibody Technique Biology Biochemistry Antibodies law.invention Adenoviridae chemistry.chemical_compound Capsid law Humans HSP70 Heat-Shock Proteins Nuclear pore Nuclear protein Hexon protein Nucleocapsid Molecular Biology In Situ Hybridization Cell Nucleus Nuclear Proteins Cell Biology Molecular biology Recombinant Proteins Cell biology Microscopy Electron chemistry DNA Viral Recombinant DNA Respiratory virus Capsid Proteins Nuclear transport Nuclear localization sequence DNA HeLa Cells |
Zdroj: | The Journal of biological chemistry. 275(6) |
ISSN: | 0021-9258 |
Popis: | Adenovirus, a respiratory virus with a double-stranded DNA genome, replicates in the nuclei of mammalian cells. We have developed a cytosol-dependent in vitro assay utilizing adenovirus nucleocapsids to examine the requirements for adenovirus docking to the nuclear pore complex and for DNA import into the nucleus. Our assay reveals that adenovirus DNA import is blocked by a competitive excess of classical protein nuclear localization sequences and other inhibitors of nuclear protein import and indicates that this process is dependent on hsc70. Previous work revealed that the hexon (coat) protein of adenovirus is the only major protein on the surface of the adenovirus nucleocapsid that docks at the nuclear pore complex. This, together with our finding that in vitro nuclear import of hexon is inhibited by an excess of classical nuclear localization sequences, suggests a role for the hexon protein in adenovirus DNA import. However, recombinant transport factors that are sufficient for hexon import in permeabilized cells do not support DNA import, indicating that there are other as yet unidentified factors required for this process. |
Databáze: | OpenAIRE |
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