A serine (threonine) protein kinase confers fungicide resistance in the phytopathogenic fungus Ustilago maydis
A mutant of Ustilago maydis (VR43) with single-gene resistance to the dicarboximide fungicide vinclozolin was previously isolated and characterized. A genomic library was constructed, and an 8.7-kb resistance-conferring fragment was isolated by sib selection. Sequencing this fragment, we identified...
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| Veröffentlicht in: | Applied and Environmental Microbiology 1995-06, Vol.61 (6), p.2341-2345 |
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| creator | Orth, A.B. (DowElanco Discovery Research, Indianapolis, IN.) Rzhetskaya, M Pell, E.J Tien, M |
| description | A mutant of Ustilago maydis (VR43) with single-gene resistance to the dicarboximide fungicide vinclozolin was previously isolated and characterized. A genomic library was constructed, and an 8.7-kb resistance-conferring fragment was isolated by sib selection. Sequencing this fragment, we identified an 1,218-bp open reading frame, which, if disrupted by deletion, no longer confers resistance. Analyses of the data in GenBank demonstrated a high degree of homology between the product of the 1,218-bp open reading frame, referred to as the adr-1 gene, and Ser (Thr) protein kinases |
| doi_str_mv | 10.1128/aem.61.6.2341-2345.1995 |
| format | Article |
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(DowElanco Discovery Research, Indianapolis, IN.) ; Rzhetskaya, M ; Pell, E.J ; Tien, M</creator><creatorcontrib>Orth, A.B. (DowElanco Discovery Research, Indianapolis, IN.) ; Rzhetskaya, M ; Pell, E.J ; Tien, M</creatorcontrib><description>A mutant of Ustilago maydis (VR43) with single-gene resistance to the dicarboximide fungicide vinclozolin was previously isolated and characterized. A genomic library was constructed, and an 8.7-kb resistance-conferring fragment was isolated by sib selection. Sequencing this fragment, we identified an 1,218-bp open reading frame, which, if disrupted by deletion, no longer confers resistance. Analyses of the data in GenBank demonstrated a high degree of homology between the product of the 1,218-bp open reading frame, referred to as the adr-1 gene, and Ser (Thr) protein kinases</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/aem.61.6.2341-2345.1995</identifier><identifier>PMID: 7793954</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DNA-Binding Proteins - genetics ; Drug Resistance, Microbial ; FONGICIDE ; Fundamental and applied biological sciences. Psychology ; Fungal plant pathogens ; Fungi ; FUNGICIDAS ; GENE ; Gene Deletion ; GENES ; Molecular Sequence Data ; Oxazoles - pharmacology ; Phytopathology. Animal pests. Plant and forest protection ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; PROTEINA QUINASA ; PROTEINE KINASE ; Proteins ; RESISTANCE AUX PRODUITS CHIMIQUES ; RESISTENCIA A PRODUCTOS QUIMICOS ; Saccharomyces cerevisiae Proteins ; SECUENCIA NUCLEICA ; Sequence Alignment ; SEQUENCE NUCLEIQUE ; Systematics. Morphology. Development cycle. Physiology ; Transcription Factors - genetics ; USTILAGO ; Ustilago - enzymology ; Ustilago - genetics ; Ustilago maydis ; VINCHLOZOLINE ; VINCLOZOLINA</subject><ispartof>Applied and Environmental Microbiology, 1995-06, Vol.61 (6), p.2341-2345</ispartof><rights>1995 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Jun 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c663t-e28ad0e49c61259706ae39aaf73e85a6ca56d76c722370d6cba549a7ddb68c743</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC167505/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC167505/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,3189,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3580353$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7793954$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orth, A.B. (DowElanco Discovery Research, Indianapolis, IN.)</creatorcontrib><creatorcontrib>Rzhetskaya, M</creatorcontrib><creatorcontrib>Pell, E.J</creatorcontrib><creatorcontrib>Tien, M</creatorcontrib><title>A serine (threonine) protein kinase confers fungicide resistance in the phytopathogenic fungus Ustilago maydis</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>A mutant of Ustilago maydis (VR43) with single-gene resistance to the dicarboximide fungicide vinclozolin was previously isolated and characterized. A genomic library was constructed, and an 8.7-kb resistance-conferring fragment was isolated by sib selection. Sequencing this fragment, we identified an 1,218-bp open reading frame, which, if disrupted by deletion, no longer confers resistance. Analyses of the data in GenBank demonstrated a high degree of homology between the product of the 1,218-bp open reading frame, referred to as the adr-1 gene, and Ser (Thr) protein kinases</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DNA-Binding Proteins - genetics</subject><subject>Drug Resistance, Microbial</subject><subject>FONGICIDE</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal plant pathogens</subject><subject>Fungi</subject><subject>FUNGICIDAS</subject><subject>GENE</subject><subject>Gene Deletion</subject><subject>GENES</subject><subject>Molecular Sequence Data</subject><subject>Oxazoles - pharmacology</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>PROTEINA QUINASA</subject><subject>PROTEINE KINASE</subject><subject>Proteins</subject><subject>RESISTANCE AUX PRODUITS CHIMIQUES</subject><subject>RESISTENCIA A PRODUCTOS QUIMICOS</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>SECUENCIA NUCLEICA</subject><subject>Sequence Alignment</subject><subject>SEQUENCE NUCLEIQUE</subject><subject>Systematics. Morphology. Development cycle. Physiology</subject><subject>Transcription Factors - genetics</subject><subject>USTILAGO</subject><subject>Ustilago - enzymology</subject><subject>Ustilago - genetics</subject><subject>Ustilago maydis</subject><subject>VINCHLOZOLINE</subject><subject>VINCLOZOLINA</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkk2P0zAQhiMEWpbCH0BCBIQQHFLs-Cs-cFit-JJW4gA9W1NnknhJ7GInoP57XFpVLJexpfd5xzN6XRTPKVlTWjfvAKe1pGu5rhmnVS5iTbUW94pLSnRTCcbk_eKSEK2ruubkYfEopVtCCCeyuSgulNJMC35Z-KsyYXQeyzfzEDH4fH1b7mKY0fnyh_OQsLTBdxhT2S2-d9a1WEZMLs3gLZYZmwcsd8N-DjuYh9Cjd_Yvu6Ryk2Y3Qh_KCfatS4-LBx2MCZ-czlWx-fjh-_Xn6ubrpy_XVzeVlZLNFdYNtAS5tpLWQisiAZkG6BTDRoC0IGSrpFV1zRRppd2C4BpU225lYxVnq-L9se9u2U7YWvRzhNHsopsg7k0AZ-4q3g2mD78MlUoQkf2vT_4Yfi6YZjO5ZHEcwWNYUsYawjlXGXz5H3gblujzbqYmQtda8cM06gjZGFKK2J0HocQc4jQ5TiOpkeYQ56EIc4gzO5_9u8fZd8ov669OOiQLYxdzJC6dMSYawvJfWBUvjtjg-uG3i2ggTXcfzczTI9NBMNDH3GbzTQtBVc3ZH54cvz4</recordid><startdate>19950601</startdate><enddate>19950601</enddate><creator>Orth, A.B. 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(DowElanco Discovery Research, Indianapolis, IN.) ; Rzhetskaya, M ; Pell, E.J ; Tien, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c663t-e28ad0e49c61259706ae39aaf73e85a6ca56d76c722370d6cba549a7ddb68c743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DNA-Binding Proteins - genetics</topic><topic>Drug Resistance, Microbial</topic><topic>FONGICIDE</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal plant pathogens</topic><topic>Fungi</topic><topic>FUNGICIDAS</topic><topic>GENE</topic><topic>Gene Deletion</topic><topic>GENES</topic><topic>Molecular Sequence Data</topic><topic>Oxazoles - pharmacology</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>PROTEINA QUINASA</topic><topic>PROTEINE KINASE</topic><topic>Proteins</topic><topic>RESISTANCE AUX PRODUITS CHIMIQUES</topic><topic>RESISTENCIA A PRODUCTOS QUIMICOS</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>SECUENCIA NUCLEICA</topic><topic>Sequence Alignment</topic><topic>SEQUENCE NUCLEIQUE</topic><topic>Systematics. Morphology. Development cycle. Physiology</topic><topic>Transcription Factors - genetics</topic><topic>USTILAGO</topic><topic>Ustilago - enzymology</topic><topic>Ustilago - genetics</topic><topic>Ustilago maydis</topic><topic>VINCHLOZOLINE</topic><topic>VINCLOZOLINA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orth, A.B. (DowElanco Discovery Research, Indianapolis, IN.)</creatorcontrib><creatorcontrib>Rzhetskaya, M</creatorcontrib><creatorcontrib>Pell, E.J</creatorcontrib><creatorcontrib>Tien, M</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orth, A.B. (DowElanco Discovery Research, Indianapolis, IN.)</au><au>Rzhetskaya, M</au><au>Pell, E.J</au><au>Tien, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A serine (threonine) protein kinase confers fungicide resistance in the phytopathogenic fungus Ustilago maydis</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>1995-06-01</date><risdate>1995</risdate><volume>61</volume><issue>6</issue><spage>2341</spage><epage>2345</epage><pages>2341-2345</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>A mutant of Ustilago maydis (VR43) with single-gene resistance to the dicarboximide fungicide vinclozolin was previously isolated and characterized. A genomic library was constructed, and an 8.7-kb resistance-conferring fragment was isolated by sib selection. Sequencing this fragment, we identified an 1,218-bp open reading frame, which, if disrupted by deletion, no longer confers resistance. Analyses of the data in GenBank demonstrated a high degree of homology between the product of the 1,218-bp open reading frame, referred to as the adr-1 gene, and Ser (Thr) protein kinases</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>7793954</pmid><doi>10.1128/aem.61.6.2341-2345.1995</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0099-2240 |
| ispartof | Applied and Environmental Microbiology, 1995-06, Vol.61 (6), p.2341-2345 |
| issn | 0099-2240 1098-5336 |
| language | eng |
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| source | MEDLINE; American Society for Microbiology Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Base Sequence Biological and medical sciences COMPOSICION QUIMICA COMPOSITION CHIMIQUE DNA-Binding Proteins - genetics Drug Resistance, Microbial FONGICIDE Fundamental and applied biological sciences. Psychology Fungal plant pathogens Fungi FUNGICIDAS GENE Gene Deletion GENES Molecular Sequence Data Oxazoles - pharmacology Phytopathology. Animal pests. Plant and forest protection Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism PROTEINA QUINASA PROTEINE KINASE Proteins RESISTANCE AUX PRODUITS CHIMIQUES RESISTENCIA A PRODUCTOS QUIMICOS Saccharomyces cerevisiae Proteins SECUENCIA NUCLEICA Sequence Alignment SEQUENCE NUCLEIQUE Systematics. Morphology. Development cycle. Physiology Transcription Factors - genetics USTILAGO Ustilago - enzymology Ustilago - genetics Ustilago maydis VINCHLOZOLINE VINCLOZOLINA |
| title | A serine (threonine) protein kinase confers fungicide resistance in the phytopathogenic fungus Ustilago maydis |
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