Involvement of a nonstructural protein in the RNA synthesis of brome mosaic virus
RNA-dependent RNA polymerase (RdRp) was prepared from brome mosaic virus (BMV)-infected barley by a procedure including Nonidet-P40 treatment. The enzyme proved to be highly active, specific, and almost completely template dependent without the need for nuclease treatment [ W. A. Miller, and T. C. H...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1988-07, Vol.165 (1), p.256-261 |
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| creator | Quadt, R. Verbeek, H.J.M. Jaspars, E.M.J. |
| description | RNA-dependent RNA polymerase (RdRp) was prepared from brome mosaic virus (BMV)-infected barley by a procedure including Nonidet-P40 treatment. The enzyme proved to be highly active, specific, and almost completely template dependent without the need for nuclease treatment [
W. A. Miller, and T. C. Hall (1983)
Virology 125, 236–241] or DEAE ion exchange chromatography [
K. Maekawa and I. Furusawa (1984)
Ann. Phytopathol. Soc. Japan 50, 491–499]. Two C-terminal peptides P1C and P2C derived from the nonstructural BMV proteins P1 and P2, respectively, were synthesized. Antibodies raised against these peptides were able to recognize the corresponding native proteins present in RdRp preparations. Antibodies directed against P1 C were capable of completely blocking the transcription of BMV RNA in vitro. This is the first experimental evidence that a nonstructural viral protein is present in an enzyme complex involved in tricornaviral RNA synthesis. |
| doi_str_mv | 10.1016/0042-6822(88)90679-4 |
| format | Article |
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W. A. Miller, and T. C. Hall (1983)
Virology 125, 236–241] or DEAE ion exchange chromatography [
K. Maekawa and I. Furusawa (1984)
Ann. Phytopathol. Soc. Japan 50, 491–499]. Two C-terminal peptides P1C and P2C derived from the nonstructural BMV proteins P1 and P2, respectively, were synthesized. Antibodies raised against these peptides were able to recognize the corresponding native proteins present in RdRp preparations. Antibodies directed against P1 C were capable of completely blocking the transcription of BMV RNA in vitro. This is the first experimental evidence that a nonstructural viral protein is present in an enzyme complex involved in tricornaviral RNA synthesis.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/0042-6822(88)90679-4</identifier><identifier>PMID: 3388771</identifier><identifier>CODEN: VIRLAX</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; ANTIBODIES ; ANTICORPS ; ANTICUERPOS ; ARN ; Biological and medical sciences ; brome mosaic virus ; Fundamental and applied biological sciences. Psychology ; HORDEUM VULGARE ; Microbiology ; Molecular Sequence Data ; Mosaic Viruses - enzymology ; Phytopathology. Animal pests. Plant and forest protection ; PLANT VIRUSES ; Plant viruses and viroids ; PROTEINAS ; PROTEINE ; PROTEINS ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; RNA ; RNA Nucleotidyltransferases - metabolism ; RNA POLYMERASE ; RNA Replicase - metabolism ; RNA, Viral - biosynthesis ; Systematics. Structure, properties and multiplication. Genetics ; TRANSFERASAS ; TRANSFERASE ; TRANSFERASES ; Viral Proteins - metabolism ; Virology ; VIRUS DE LAS PLANTAS ; VIRUS DES VEGETAUX</subject><ispartof>Virology (New York, N.Y.), 1988-07, Vol.165 (1), p.256-261</ispartof><rights>1988</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c436t-a086798aa467aa18dff0bb0ffe4cd7813cfdb537c4bdfe35222f62392891ba1e3</citedby><cites>FETCH-LOGICAL-c436t-a086798aa467aa18dff0bb0ffe4cd7813cfdb537c4bdfe35222f62392891ba1e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0042-6822(88)90679-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7101327$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3388771$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quadt, R.</creatorcontrib><creatorcontrib>Verbeek, H.J.M.</creatorcontrib><creatorcontrib>Jaspars, E.M.J.</creatorcontrib><title>Involvement of a nonstructural protein in the RNA synthesis of brome mosaic virus</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>RNA-dependent RNA polymerase (RdRp) was prepared from brome mosaic virus (BMV)-infected barley by a procedure including Nonidet-P40 treatment. The enzyme proved to be highly active, specific, and almost completely template dependent without the need for nuclease treatment [
W. A. Miller, and T. C. Hall (1983)
Virology 125, 236–241] or DEAE ion exchange chromatography [
K. Maekawa and I. Furusawa (1984)
Ann. Phytopathol. Soc. Japan 50, 491–499]. Two C-terminal peptides P1C and P2C derived from the nonstructural BMV proteins P1 and P2, respectively, were synthesized. Antibodies raised against these peptides were able to recognize the corresponding native proteins present in RdRp preparations. Antibodies directed against P1 C were capable of completely blocking the transcription of BMV RNA in vitro. This is the first experimental evidence that a nonstructural viral protein is present in an enzyme complex involved in tricornaviral RNA synthesis.</description><subject>Amino Acid Sequence</subject><subject>ANTIBODIES</subject><subject>ANTICORPS</subject><subject>ANTICUERPOS</subject><subject>ARN</subject><subject>Biological and medical sciences</subject><subject>brome mosaic virus</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HORDEUM VULGARE</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mosaic Viruses - enzymology</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>PLANT VIRUSES</subject><subject>Plant viruses and viroids</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>RNA</subject><subject>RNA Nucleotidyltransferases - metabolism</subject><subject>RNA POLYMERASE</subject><subject>RNA Replicase - metabolism</subject><subject>RNA, Viral - biosynthesis</subject><subject>Systematics. Structure, properties and multiplication. Genetics</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>TRANSFERASES</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><subject>VIRUS DE LAS PLANTAS</subject><subject>VIRUS DES VEGETAUX</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF1rFDEUhkNR6rb2D4hCLqTUi9F8bZK5EUppa6EorfY6ZDInGplJ2mRmof_ejLvspUIgCe9zDi8PQm8p-UgJlZ8IEayRmrEzrT-0RKq2EQdoRUkrG8IFfYFWe-QVOirlN6l_pcghOuRca6XoCt3dxE0aNjBCnHDy2OKYYpny7KY52wE_5jRBiLie6Rfg-6_nuDzH-iyhLHyX0wh4TMUGhzchz-U1euntUOBkdx-jh6vLHxdfmttv1zcX57eNE1xOjSW6NtbWCqmspbr3nnQd8R6E65Wm3Pm-W3PlRNd74GvGmJeMt0y3tLMU-DE63e6tFZ9mKJMZQ3EwDDZCmotRmrWMM_pfkIpWMtUuoNiCLqdSMnjzmMNo87OhxCzKzeLTLD6N1uavciPq2Lvd_rkbod8P7RzX_P0ut8XZwWcbXSh7TNXNnKmKvdli3iZjf-aKPHzXei0klzX8vA2hGt0EyKa4ANFBHzK4yfQp_LvkH7FXpU8</recordid><startdate>19880701</startdate><enddate>19880701</enddate><creator>Quadt, R.</creator><creator>Verbeek, H.J.M.</creator><creator>Jaspars, E.M.J.</creator><general>Elsevier Inc</general><general>Elsevier</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>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19880701</creationdate><title>Involvement of a nonstructural protein in the RNA synthesis of brome mosaic virus</title><author>Quadt, R. ; Verbeek, H.J.M. ; Jaspars, E.M.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-a086798aa467aa18dff0bb0ffe4cd7813cfdb537c4bdfe35222f62392891ba1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>ANTIBODIES</topic><topic>ANTICORPS</topic><topic>ANTICUERPOS</topic><topic>ARN</topic><topic>Biological and medical sciences</topic><topic>brome mosaic virus</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HORDEUM VULGARE</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mosaic Viruses - enzymology</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>PLANT VIRUSES</topic><topic>Plant viruses and viroids</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>RNA</topic><topic>RNA Nucleotidyltransferases - metabolism</topic><topic>RNA POLYMERASE</topic><topic>RNA Replicase - metabolism</topic><topic>RNA, Viral - biosynthesis</topic><topic>Systematics. Structure, properties and multiplication. Genetics</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>TRANSFERASES</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><topic>VIRUS DE LAS PLANTAS</topic><topic>VIRUS DES VEGETAUX</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quadt, R.</creatorcontrib><creatorcontrib>Verbeek, H.J.M.</creatorcontrib><creatorcontrib>Jaspars, E.M.J.</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>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quadt, R.</au><au>Verbeek, H.J.M.</au><au>Jaspars, E.M.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of a nonstructural protein in the RNA synthesis of brome mosaic virus</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1988-07-01</date><risdate>1988</risdate><volume>165</volume><issue>1</issue><spage>256</spage><epage>261</epage><pages>256-261</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>RNA-dependent RNA polymerase (RdRp) was prepared from brome mosaic virus (BMV)-infected barley by a procedure including Nonidet-P40 treatment. The enzyme proved to be highly active, specific, and almost completely template dependent without the need for nuclease treatment [
W. A. Miller, and T. C. Hall (1983)
Virology 125, 236–241] or DEAE ion exchange chromatography [
K. Maekawa and I. Furusawa (1984)
Ann. Phytopathol. Soc. Japan 50, 491–499]. Two C-terminal peptides P1C and P2C derived from the nonstructural BMV proteins P1 and P2, respectively, were synthesized. Antibodies raised against these peptides were able to recognize the corresponding native proteins present in RdRp preparations. Antibodies directed against P1 C were capable of completely blocking the transcription of BMV RNA in vitro. This is the first experimental evidence that a nonstructural viral protein is present in an enzyme complex involved in tricornaviral RNA synthesis.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3388771</pmid><doi>10.1016/0042-6822(88)90679-4</doi><tpages>6</tpages></addata></record> |
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| ispartof | Virology (New York, N.Y.), 1988-07, Vol.165 (1), p.256-261 |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence ANTIBODIES ANTICORPS ANTICUERPOS ARN Biological and medical sciences brome mosaic virus Fundamental and applied biological sciences. Psychology HORDEUM VULGARE Microbiology Molecular Sequence Data Mosaic Viruses - enzymology Phytopathology. Animal pests. Plant and forest protection PLANT VIRUSES Plant viruses and viroids PROTEINAS PROTEINE PROTEINS Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains RNA RNA Nucleotidyltransferases - metabolism RNA POLYMERASE RNA Replicase - metabolism RNA, Viral - biosynthesis Systematics. Structure, properties and multiplication. Genetics TRANSFERASAS TRANSFERASE TRANSFERASES Viral Proteins - metabolism Virology VIRUS DE LAS PLANTAS VIRUS DES VEGETAUX |
| title | Involvement of a nonstructural protein in the RNA synthesis of brome mosaic virus |
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