Regulated nuclear targeting of cauliflower mosaic virus
The mature cauliflower mosaic virus (CaMV) capsid protein (CP), if expressed in the absence of other viral proteins, is transported into the plant cell nucleus by the action of a nuclear localization signal (NLS) close to the N terminus. In contrast, virus particles do not enter the nucleus, but doc...
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| Veröffentlicht in: | Journal of general virology 2002-07, Vol.83 (7), p.1783-1790 |
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| container_issue | 7 |
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| container_title | Journal of general virology |
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| creator | Karsies, A Merkle, T Szurek, B Bonas, U Hohn, T Leclerc, D |
| description | The mature cauliflower mosaic virus (CaMV) capsid protein (CP), if expressed in the absence of other viral proteins, is transported into the plant cell nucleus by the action of a nuclear localization signal (NLS) close to the N terminus. In contrast, virus particles do not enter the nucleus, but dock et the nuclear membrane, a process inhibited by anti-NLS antibodies or by GTPgammaS, and apparently mediated by interaction of CP with host importin alpha. The very acidic N-terminal extension of the viral CP precursor inhibits nuclear targeting of the protein and hence the precursor is localized in the cytoplasm. We hypothesize that this provides a control mechanism which ensures that the CP precursor is used for virus assembly in the cytoplasm and that only mature virus particles reach the nuclear pore. |
| doi_str_mv | 10.1099/0022-1317-83-7-1783 |
| format | Article |
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In contrast, virus particles do not enter the nucleus, but dock et the nuclear membrane, a process inhibited by anti-NLS antibodies or by GTPgammaS, and apparently mediated by interaction of CP with host importin alpha. The very acidic N-terminal extension of the viral CP precursor inhibits nuclear targeting of the protein and hence the precursor is localized in the cytoplasm. 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In contrast, virus particles do not enter the nucleus, but dock et the nuclear membrane, a process inhibited by anti-NLS antibodies or by GTPgammaS, and apparently mediated by interaction of CP with host importin alpha. The very acidic N-terminal extension of the viral CP precursor inhibits nuclear targeting of the protein and hence the precursor is localized in the cytoplasm. We hypothesize that this provides a control mechanism which ensures that the CP precursor is used for virus assembly in the cytoplasm and that only mature virus particles reach the nuclear pore.</description><subject>Amino Acid Sequence</subject><subject>antibodies</subject><subject>Antibodies - pharmacology</subject><subject>Blotting, Western</subject><subject>Capsid - genetics</subject><subject>Capsid - metabolism</subject><subject>Capsid - pharmacology</subject><subject>Cauliflower mosaic virus</subject><subject>Caulimovirus - isolation & purification</subject><subject>Caulimovirus - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>coat proteins</subject><subject>cytoplasm</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - metabolism</subject><subject>importins</subject><subject>Karyopherins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nicotiana - genetics</subject><subject>Nuclear Envelope - virology</subject><subject>Nuclear Localization Signals</subject><subject>nuclear membrane</subject><subject>Protein Binding</subject><subject>Terminal Repeat Sequences</subject><subject>Transfection</subject><subject>virion</subject><subject>Virus Assembly</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkE1LxDAQQIMo7rr6CwTtSbxUJ52kaY-y-AULgrrnkE2TbqQfa9K6-O_t0kU9zWHevIFHyDmFGwp5fguQJDFFKuIMYxFTkeEBmVKW8jgZ9odk-ktMyEkIHwCUMS6OyYQmIDgFmBLxasq-Up0poqbXlVE-6pQvTeeaMmptpFVfOVu1W-Ojug3K6ejL-T6ckiOrqmDO9nNGlg_37_OnePHy-Dy_W8SaAXaxRUCqAbVACgUgMM6tTjgWwESqVykktuA0tRkrQK1MzrLU8oypXBlh8hRn5Gr0bnz72ZvQydoFbapKNabtgxQ0Q54LGEAcQe3bELyxcuNdrfy3pCB3veSuhtzVkBlKIXe9hquLvb5f1ab4u9kHGoDrEVi7cr113sjSNLUbnqxcK4cU_12XI2pVK1XpXZDLtwRoCjDIOCL-ABMUe98</recordid><startdate>20020701</startdate><enddate>20020701</enddate><creator>Karsies, A</creator><creator>Merkle, T</creator><creator>Szurek, B</creator><creator>Bonas, U</creator><creator>Hohn, T</creator><creator>Leclerc, D</creator><general>Soc General Microbiol</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020701</creationdate><title>Regulated nuclear targeting of cauliflower mosaic virus</title><author>Karsies, A ; 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| ispartof | Journal of general virology, 2002-07, Vol.83 (7), p.1783-1790 |
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| language | eng |
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| source | MEDLINE; Microbiology Society; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence antibodies Antibodies - pharmacology Blotting, Western Capsid - genetics Capsid - metabolism Capsid - pharmacology Cauliflower mosaic virus Caulimovirus - isolation & purification Caulimovirus - metabolism Cell Nucleus - metabolism coat proteins cytoplasm Guanosine 5'-O-(3-Thiotriphosphate) - metabolism importins Karyopherins - metabolism Molecular Sequence Data Mutation Nicotiana - genetics Nuclear Envelope - virology Nuclear Localization Signals nuclear membrane Protein Binding Terminal Repeat Sequences Transfection virion Virus Assembly |
| title | Regulated nuclear targeting of cauliflower mosaic virus |
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