Molecular characterization of the genome of a partitivirus from the basidiomycete Rhizoctonia solani
Department of Biological Sciences, University of Maine, Orono, ME 04469-0102, USA 1 Author for correspondence: Stellos Tavantzis. Fax +1 207 581 2969. e-mail stellos{at}umit.maine.edu The bisegmented genome of a double-stranded (ds) RNA virus from the fungus Rhizoctonia solani isolate Rhs 717 was ch...
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creator | Strauss, Ethan E Lakshman, Dilip K Tavantzis, Stellos M |
description | Department of Biological Sciences, University of Maine, Orono, ME 04469-0102, USA 1
Author for correspondence: Stellos Tavantzis. Fax +1 207 581 2969. e-mail stellos{at}umit.maine.edu
The bisegmented genome of a double-stranded (ds) RNA virus from the fungus Rhizoctonia solani isolate Rhs 717 was characterized. The larger segment, dsRNA 1, is 2363 bases long whereas the smaller segment, dsRNA 2, has 2206 bases. The 5' ends of the coding strands of dsRNA 1 and dsRNA 2 are highly conserved (100% identity over 47 bases), and contain inverted repeats capable of forming stable stemloop structures. Analysis of the coding potential of each of the two segments showed that dsRNAs 1 and 2 could code for polypeptides of 730 aa (bases 862275; molecular mass 86 kDa) and 683 aa (bases 792130; molecular mass 76 kDa), respectively. The 86 kDa polypeptide has all the motifs of dsRNA RNA-dependent RNA polymerases (RDRP), and has significant homology with putative RDRPs of partitiviruses from Fusarium poae and Atkinsonella hypoxylon . The 76 kDa protein shows homology with the putative capsid proteins (CP) of the same viruses. Northern blot analysis revealed no subgenomic RNA species, consistent with the fact that the long open reading frames encoding the putative RDRP and CP cover the entire length of the respective dsRNAs. |
doi_str_mv | 10.1099/0022-1317-81-2-549 |
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Author for correspondence: Stellos Tavantzis. Fax +1 207 581 2969. e-mail stellos{at}umit.maine.edu
The bisegmented genome of a double-stranded (ds) RNA virus from the fungus Rhizoctonia solani isolate Rhs 717 was characterized. The larger segment, dsRNA 1, is 2363 bases long whereas the smaller segment, dsRNA 2, has 2206 bases. The 5' ends of the coding strands of dsRNA 1 and dsRNA 2 are highly conserved (100% identity over 47 bases), and contain inverted repeats capable of forming stable stemloop structures. Analysis of the coding potential of each of the two segments showed that dsRNAs 1 and 2 could code for polypeptides of 730 aa (bases 862275; molecular mass 86 kDa) and 683 aa (bases 792130; molecular mass 76 kDa), respectively. The 86 kDa polypeptide has all the motifs of dsRNA RNA-dependent RNA polymerases (RDRP), and has significant homology with putative RDRPs of partitiviruses from Fusarium poae and Atkinsonella hypoxylon . The 76 kDa protein shows homology with the putative capsid proteins (CP) of the same viruses. Northern blot analysis revealed no subgenomic RNA species, consistent with the fact that the long open reading frames encoding the putative RDRP and CP cover the entire length of the respective dsRNAs.</description><identifier>ISSN: 0022-1317</identifier><identifier>ISSN: 1350-0872</identifier><identifier>EISSN: 1465-2099</identifier><identifier>EISSN: 1465-2080</identifier><identifier>DOI: 10.1099/0022-1317-81-2-549</identifier><identifier>PMID: 10644855</identifier><language>eng</language><publisher>England: Soc General Microbiol</publisher><subject>Amino Acid Sequence ; Atkinsonella hypoxylon ; Base Sequence ; Basidiomycota - virology ; Capsid - genetics ; DNA Primers - genetics ; Fusarium poae ; Gene Expression ; Genome, Viral ; Molecular Sequence Data ; Molecular Weight ; Partitivirus ; Phylogeny ; Rhizoctonia solani ; RNA Replicase - genetics ; RNA Viruses - classification ; RNA Viruses - genetics ; RNA Viruses - isolation & purification ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; Viral Proteins - chemistry ; Viral Proteins - genetics</subject><ispartof>Journal of general virology, 2000-02, Vol.81 (2), p.549-555</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-f7ffccd6526f6edda2f6e53eea305ed5aad84b4b3640059933cb2822b4f849863</citedby><cites>FETCH-LOGICAL-c397t-f7ffccd6526f6edda2f6e53eea305ed5aad84b4b3640059933cb2822b4f849863</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3747,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10644855$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Strauss, Ethan E</creatorcontrib><creatorcontrib>Lakshman, Dilip K</creatorcontrib><creatorcontrib>Tavantzis, Stellos M</creatorcontrib><title>Molecular characterization of the genome of a partitivirus from the basidiomycete Rhizoctonia solani</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>Department of Biological Sciences, University of Maine, Orono, ME 04469-0102, USA 1
Author for correspondence: Stellos Tavantzis. Fax +1 207 581 2969. e-mail stellos{at}umit.maine.edu
The bisegmented genome of a double-stranded (ds) RNA virus from the fungus Rhizoctonia solani isolate Rhs 717 was characterized. The larger segment, dsRNA 1, is 2363 bases long whereas the smaller segment, dsRNA 2, has 2206 bases. The 5' ends of the coding strands of dsRNA 1 and dsRNA 2 are highly conserved (100% identity over 47 bases), and contain inverted repeats capable of forming stable stemloop structures. Analysis of the coding potential of each of the two segments showed that dsRNAs 1 and 2 could code for polypeptides of 730 aa (bases 862275; molecular mass 86 kDa) and 683 aa (bases 792130; molecular mass 76 kDa), respectively. The 86 kDa polypeptide has all the motifs of dsRNA RNA-dependent RNA polymerases (RDRP), and has significant homology with putative RDRPs of partitiviruses from Fusarium poae and Atkinsonella hypoxylon . The 76 kDa protein shows homology with the putative capsid proteins (CP) of the same viruses. Northern blot analysis revealed no subgenomic RNA species, consistent with the fact that the long open reading frames encoding the putative RDRP and CP cover the entire length of the respective dsRNAs.</description><subject>Amino Acid Sequence</subject><subject>Atkinsonella hypoxylon</subject><subject>Base Sequence</subject><subject>Basidiomycota - virology</subject><subject>Capsid - genetics</subject><subject>DNA Primers - genetics</subject><subject>Fusarium poae</subject><subject>Gene Expression</subject><subject>Genome, Viral</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Partitivirus</subject><subject>Phylogeny</subject><subject>Rhizoctonia solani</subject><subject>RNA Replicase - genetics</subject><subject>RNA Viruses - classification</subject><subject>RNA Viruses - genetics</subject><subject>RNA Viruses - isolation & purification</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><issn>0022-1317</issn><issn>1350-0872</issn><issn>1465-2099</issn><issn>1465-2080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkE1LxDAQhoMo7vrxBzxIT3qqJmmStkcRv2BFED2HNJ1sI-1mTVJl_fVm3WXxNAzzzDvDg9AZwVcE1_U1xpTmpCBlXpGc5pzVe2hKmOA5TeN9NN0BE3QUwgfGhDFeHqIJwYKxivMpap9dD3rslc90p7zSEbz9UdG6ReZMFjvI5rBwA6w7lS2VjzbaL-vHkBnvhj-iUcG21g0rDRGy187-OB3dwqosuF4t7Ak6MKoPcLqtx-j9_u7t9jGfvTw83d7Mcl3UZcxNaYzWreBUGAFtq2gqvABQBebQcqXaijWsKQTDmNd1UeiGVpQ2zFSsrkRxjC42uUvvPkcIUQ42aOjTD-DGIEnJSsEFTSDdgNq7EDwYufR2UH4lCZZrt3KtTq7VyYpIKpPbtHS-TR-bAdp_KxuZCbjcAJ2dd9_Wg0zqBptuNNbJ5GwX9Qs-1YS9</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Strauss, Ethan E</creator><creator>Lakshman, Dilip K</creator><creator>Tavantzis, Stellos M</creator><general>Soc General Microbiol</general><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>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20000201</creationdate><title>Molecular characterization of the genome of a partitivirus from the basidiomycete Rhizoctonia solani</title><author>Strauss, Ethan E ; Lakshman, Dilip K ; Tavantzis, Stellos M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-f7ffccd6526f6edda2f6e53eea305ed5aad84b4b3640059933cb2822b4f849863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Atkinsonella hypoxylon</topic><topic>Base Sequence</topic><topic>Basidiomycota - virology</topic><topic>Capsid - genetics</topic><topic>DNA Primers - genetics</topic><topic>Fusarium poae</topic><topic>Gene Expression</topic><topic>Genome, Viral</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Partitivirus</topic><topic>Phylogeny</topic><topic>Rhizoctonia solani</topic><topic>RNA Replicase - genetics</topic><topic>RNA Viruses - classification</topic><topic>RNA Viruses - genetics</topic><topic>RNA Viruses - isolation & purification</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strauss, Ethan E</creatorcontrib><creatorcontrib>Lakshman, Dilip K</creatorcontrib><creatorcontrib>Tavantzis, Stellos M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strauss, Ethan E</au><au>Lakshman, Dilip K</au><au>Tavantzis, Stellos M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of the genome of a partitivirus from the basidiomycete Rhizoctonia solani</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>81</volume><issue>2</issue><spage>549</spage><epage>555</epage><pages>549-555</pages><issn>0022-1317</issn><issn>1350-0872</issn><eissn>1465-2099</eissn><eissn>1465-2080</eissn><abstract>Department of Biological Sciences, University of Maine, Orono, ME 04469-0102, USA 1
Author for correspondence: Stellos Tavantzis. Fax +1 207 581 2969. e-mail stellos{at}umit.maine.edu
The bisegmented genome of a double-stranded (ds) RNA virus from the fungus Rhizoctonia solani isolate Rhs 717 was characterized. The larger segment, dsRNA 1, is 2363 bases long whereas the smaller segment, dsRNA 2, has 2206 bases. The 5' ends of the coding strands of dsRNA 1 and dsRNA 2 are highly conserved (100% identity over 47 bases), and contain inverted repeats capable of forming stable stemloop structures. Analysis of the coding potential of each of the two segments showed that dsRNAs 1 and 2 could code for polypeptides of 730 aa (bases 862275; molecular mass 86 kDa) and 683 aa (bases 792130; molecular mass 76 kDa), respectively. The 86 kDa polypeptide has all the motifs of dsRNA RNA-dependent RNA polymerases (RDRP), and has significant homology with putative RDRPs of partitiviruses from Fusarium poae and Atkinsonella hypoxylon . The 76 kDa protein shows homology with the putative capsid proteins (CP) of the same viruses. Northern blot analysis revealed no subgenomic RNA species, consistent with the fact that the long open reading frames encoding the putative RDRP and CP cover the entire length of the respective dsRNAs.</abstract><cop>England</cop><pub>Soc General Microbiol</pub><pmid>10644855</pmid><doi>10.1099/0022-1317-81-2-549</doi><tpages>7</tpages></addata></record> |
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subjects | Amino Acid Sequence Atkinsonella hypoxylon Base Sequence Basidiomycota - virology Capsid - genetics DNA Primers - genetics Fusarium poae Gene Expression Genome, Viral Molecular Sequence Data Molecular Weight Partitivirus Phylogeny Rhizoctonia solani RNA Replicase - genetics RNA Viruses - classification RNA Viruses - genetics RNA Viruses - isolation & purification Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Viral Proteins - chemistry Viral Proteins - genetics |
title | Molecular characterization of the genome of a partitivirus from the basidiomycete Rhizoctonia solani |
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