Biological functions of the cytoplasmic TGBp1 inclusions of bamboo mosaic potexvirus
The TGBp1 protein encoded by the first open reading frame of the triple-gene-block (TGB) of bamboo mosaic potexvirus (BaMV) plays important roles in virus movement; one of them is to shape the viral RNA before its being transported from cell to cell. However, TGBp1 mainly forms cytoplasmic inclusion...
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| Veröffentlicht in: | Archives of virology 2004-05, Vol.149 (5), p.1027-1035 |
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| creator | Hsu, H.T Hsu, Y.H Bi, I.P Lin, N.S Chang, B.Y |
| description | The TGBp1 protein encoded by the first open reading frame of the triple-gene-block (TGB) of bamboo mosaic potexvirus (BaMV) plays important roles in virus movement; one of them is to shape the viral RNA before its being transported from cell to cell. However, TGBp1 mainly forms cytoplasmic inclusions which are devoid of the RNA-binding activity. With the purified TGBp1 inclusions of BaMV, we analyzed the possibility of dissociation of functional TGBp1 from the inclusions. Our data showed that the cytoplasmic inclusions were able to dissociate continuously functional TGBp1, which possessed ATP-binding, ATPase, and RNA-binding activities. Moreover, the dissociation of TGBp1 was significantly enhanced by the presence of viral RNA and capsid protein (CP), consistent with the finding that TGBp1 are able to form ribonucleoprotein complex with viral RNA and CP. Taken together, these results support the idea that the cytoplasmic TGBp1 inclusions are active pools of TGBp1, upon which viral RNA can be shaped into a transferable form. |
| doi_str_mv | 10.1007/s00705-003-0254-y |
| format | Article |
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However, TGBp1 mainly forms cytoplasmic inclusions which are devoid of the RNA-binding activity. With the purified TGBp1 inclusions of BaMV, we analyzed the possibility of dissociation of functional TGBp1 from the inclusions. Our data showed that the cytoplasmic inclusions were able to dissociate continuously functional TGBp1, which possessed ATP-binding, ATPase, and RNA-binding activities. Moreover, the dissociation of TGBp1 was significantly enhanced by the presence of viral RNA and capsid protein (CP), consistent with the finding that TGBp1 are able to form ribonucleoprotein complex with viral RNA and CP. Taken together, these results support the idea that the cytoplasmic TGBp1 inclusions are active pools of TGBp1, upon which viral RNA can be shaped into a transferable form.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-003-0254-y</identifier><identifier>PMID: 15098116</identifier><language>eng</language><publisher>Wien: Springer</publisher><subject>Adenosine Triphosphatases - metabolism ; Adenosine Triphosphate - metabolism ; bamboo mosaic potexvirus ; Bamboo mosaic virus ; Biological and medical sciences ; Chenopodium quinoa - metabolism ; Chenopodium quinoa - virology ; cytoplasmic inclusions ; Fundamental and applied biological sciences. Psychology ; Human viral diseases ; Inclusion Bodies - metabolism ; Infectious diseases ; Medical sciences ; Microbiology ; Miscellaneous ; Plant Viral Movement Proteins ; Potexvirus - metabolism ; Protein Binding ; Proteins ; RNA polymerase ; RNA, Viral - metabolism ; TGBp1 protein ; triple gene block protein 1 ; Viral diseases ; viral proteins ; Viral Proteins - metabolism ; Virology ; Viruses</subject><ispartof>Archives of virology, 2004-05, Vol.149 (5), p.1027-1035</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Springer-Verlag 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-2eda26932ac15f77222327d708d49ce551e71f47fa422b52f533ac87699c1ecc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15752389$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15098116$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hsu, H.T</creatorcontrib><creatorcontrib>Hsu, Y.H</creatorcontrib><creatorcontrib>Bi, I.P</creatorcontrib><creatorcontrib>Lin, N.S</creatorcontrib><creatorcontrib>Chang, B.Y</creatorcontrib><title>Biological functions of the cytoplasmic TGBp1 inclusions of bamboo mosaic potexvirus</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><description>The TGBp1 protein encoded by the first open reading frame of the triple-gene-block (TGB) of bamboo mosaic potexvirus (BaMV) plays important roles in virus movement; one of them is to shape the viral RNA before its being transported from cell to cell. However, TGBp1 mainly forms cytoplasmic inclusions which are devoid of the RNA-binding activity. With the purified TGBp1 inclusions of BaMV, we analyzed the possibility of dissociation of functional TGBp1 from the inclusions. Our data showed that the cytoplasmic inclusions were able to dissociate continuously functional TGBp1, which possessed ATP-binding, ATPase, and RNA-binding activities. Moreover, the dissociation of TGBp1 was significantly enhanced by the presence of viral RNA and capsid protein (CP), consistent with the finding that TGBp1 are able to form ribonucleoprotein complex with viral RNA and CP. Taken together, these results support the idea that the cytoplasmic TGBp1 inclusions are active pools of TGBp1, upon which viral RNA can be shaped into a transferable form.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>bamboo mosaic potexvirus</subject><subject>Bamboo mosaic virus</subject><subject>Biological and medical sciences</subject><subject>Chenopodium quinoa - metabolism</subject><subject>Chenopodium quinoa - virology</subject><subject>cytoplasmic inclusions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Human viral diseases</subject><subject>Inclusion Bodies - metabolism</subject><subject>Infectious diseases</subject><subject>Medical sciences</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Plant Viral Movement Proteins</subject><subject>Potexvirus - metabolism</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>RNA polymerase</subject><subject>RNA, Viral - metabolism</subject><subject>TGBp1 protein</subject><subject>triple gene block protein 1</subject><subject>Viral diseases</subject><subject>viral proteins</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><subject>Viruses</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0U1v1DAQBmCrAtGl8AN6aSMkuAVm_BHbR1pBQarEge3Z8nrt1lUSBztB7L_H1W5F1QsXz-WZGXleQk4RPiKA_FTqA6IFYC1QwdvdEVkhZ7RVUqsXZAUMeKs6UMfkdSn3UCEw8YocowCtELsVWV_E1Kfb6GzfhGV0c0xjaVJo5jvfuN2cpt6WIbpmfXUxYRNH1y_l0WzssEmpGVKxVUxp9n9-x7yUN-RlsH3xbw_1hNx8_bK-_NZe_7j6fvn5unUc9NxSv7W004xahyJISSllVG4lqC3XzguBXmLgMlhO6UbQIBizTslOa4feOXZCPuznTjn9WnyZzRCL831vR5-WYiQqzjqg_4UoNZOaQoXvnsH7tOSxfsJQpEx1mncV4R65nErJPpgpx8HmnUEwD8GYfTCm3ts8BGN2tefsMHjZDH77r-OQRAXvD8CWGkbIdnSxPHFS1P26uvO9CzYZe5uruflJARmAlqDrif4C8GWeOA</recordid><startdate>20040501</startdate><enddate>20040501</enddate><creator>Hsu, H.T</creator><creator>Hsu, Y.H</creator><creator>Bi, I.P</creator><creator>Lin, N.S</creator><creator>Chang, B.Y</creator><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040501</creationdate><title>Biological functions of the cytoplasmic TGBp1 inclusions of bamboo mosaic potexvirus</title><author>Hsu, H.T ; Hsu, Y.H ; Bi, I.P ; Lin, N.S ; Chang, B.Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-2eda26932ac15f77222327d708d49ce551e71f47fa422b52f533ac87699c1ecc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>bamboo mosaic potexvirus</topic><topic>Bamboo mosaic virus</topic><topic>Biological and medical sciences</topic><topic>Chenopodium quinoa - metabolism</topic><topic>Chenopodium quinoa - virology</topic><topic>cytoplasmic inclusions</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Human viral diseases</topic><topic>Inclusion Bodies - metabolism</topic><topic>Infectious diseases</topic><topic>Medical sciences</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Plant Viral Movement Proteins</topic><topic>Potexvirus - metabolism</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>RNA polymerase</topic><topic>RNA, Viral - metabolism</topic><topic>TGBp1 protein</topic><topic>triple gene block protein 1</topic><topic>Viral diseases</topic><topic>viral proteins</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hsu, H.T</creatorcontrib><creatorcontrib>Hsu, Y.H</creatorcontrib><creatorcontrib>Bi, I.P</creatorcontrib><creatorcontrib>Lin, N.S</creatorcontrib><creatorcontrib>Chang, B.Y</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hsu, H.T</au><au>Hsu, Y.H</au><au>Bi, I.P</au><au>Lin, N.S</au><au>Chang, B.Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biological functions of the cytoplasmic TGBp1 inclusions of bamboo mosaic potexvirus</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>2004-05-01</date><risdate>2004</risdate><volume>149</volume><issue>5</issue><spage>1027</spage><epage>1035</epage><pages>1027-1035</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>The TGBp1 protein encoded by the first open reading frame of the triple-gene-block (TGB) of bamboo mosaic potexvirus (BaMV) plays important roles in virus movement; one of them is to shape the viral RNA before its being transported from cell to cell. However, TGBp1 mainly forms cytoplasmic inclusions which are devoid of the RNA-binding activity. With the purified TGBp1 inclusions of BaMV, we analyzed the possibility of dissociation of functional TGBp1 from the inclusions. Our data showed that the cytoplasmic inclusions were able to dissociate continuously functional TGBp1, which possessed ATP-binding, ATPase, and RNA-binding activities. Moreover, the dissociation of TGBp1 was significantly enhanced by the presence of viral RNA and capsid protein (CP), consistent with the finding that TGBp1 are able to form ribonucleoprotein complex with viral RNA and CP. Taken together, these results support the idea that the cytoplasmic TGBp1 inclusions are active pools of TGBp1, upon which viral RNA can be shaped into a transferable form.</abstract><cop>Wien</cop><cop>New York, NY</cop><pub>Springer</pub><pmid>15098116</pmid><doi>10.1007/s00705-003-0254-y</doi><tpages>9</tpages></addata></record> |
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| subjects | Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism bamboo mosaic potexvirus Bamboo mosaic virus Biological and medical sciences Chenopodium quinoa - metabolism Chenopodium quinoa - virology cytoplasmic inclusions Fundamental and applied biological sciences. Psychology Human viral diseases Inclusion Bodies - metabolism Infectious diseases Medical sciences Microbiology Miscellaneous Plant Viral Movement Proteins Potexvirus - metabolism Protein Binding Proteins RNA polymerase RNA, Viral - metabolism TGBp1 protein triple gene block protein 1 Viral diseases viral proteins Viral Proteins - metabolism Virology Viruses |
| title | Biological functions of the cytoplasmic TGBp1 inclusions of bamboo mosaic potexvirus |
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