Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi
Oomycetes from the genus Phytophthora are fungus-like plant pathogens that are devastating for agriculture and natural ecosystems. They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One o...
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| Veröffentlicht in: | Molecular biology reports 2014, Vol.41 (4), p.2453-2462 |
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| creator | Martins, Ivone M Martins, Fátima Belo, Hélio Vaz, Madalena Carvalho, Marisa Cravador, Alfredo Choupina, Altino |
| description | Oomycetes from the genus Phytophthora are fungus-like plant pathogens that are devastating for agriculture and natural ecosystems. They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One of the most widely distributed and aggressive Phytophthora species, with more than 1,000 host plants is P. cinnamomi. In this work we report the sequencing and characterization of a class of GIPs secreted by Phytophthora cinnamomi. The gip gene from P. cinnamomi has a 937 bp ORF encoding a putative peptide of 312 deduced amino acids. The expression of this gene was studied during growth in different carbon sources (glucose, cellulose and sawdust), by RT-qPCR and its level of expression was evaluated at five time points. The highest expression of gip gene occurred in sawdust at 8 h of induction. In vivo infection of C. sativa revealed an increase in gip expression from 12 to 24 h. At 36 h its expression decreased suggesting that a compensatory mechanism must occur in plant. |
| doi_str_mv | 10.1007/s11033-014-3101-1 |
| format | Article |
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They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One of the most widely distributed and aggressive Phytophthora species, with more than 1,000 host plants is P. cinnamomi. In this work we report the sequencing and characterization of a class of GIPs secreted by Phytophthora cinnamomi. The gip gene from P. cinnamomi has a 937 bp ORF encoding a putative peptide of 312 deduced amino acids. The expression of this gene was studied during growth in different carbon sources (glucose, cellulose and sawdust), by RT-qPCR and its level of expression was evaluated at five time points. The highest expression of gip gene occurred in sawdust at 8 h of induction. In vivo infection of C. sativa revealed an increase in gip expression from 12 to 24 h. At 36 h its expression decreased suggesting that a compensatory mechanism must occur in plant.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-014-3101-1</identifier><identifier>PMID: 24420864</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Amino Acid Sequence ; amino acids ; Animal Anatomy ; Animal Biochemistry ; Biomedical and Life Sciences ; Cannabis - genetics ; carbon ; cellulose ; Cloning, Molecular ; ecosystems ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Gene Expression ; genes ; glucose ; Histology ; host plants ; Life Sciences ; Models, Molecular ; Molecular biology ; Molecular Sequence Data ; Morphology ; Oomycetes ; open reading frames ; Pathogens ; Phenotype ; Phytophthora ; Phytophthora - genetics ; Phytophthora cinnamomi ; Plant diseases ; Plant Diseases - microbiology ; plant pathogens ; Plant Roots - microbiology ; Polymerase chain reaction ; Protein Conformation ; Proteins ; sawdust ; Time Factors</subject><ispartof>Molecular biology reports, 2014, Vol.41 (4), p.2453-2462</ispartof><rights>Springer Science+Business Media Dordrecht 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-9dd472ad5f5cfe50171126d782a061fbe572775c8171ef64fe2475327f255da13</citedby><cites>FETCH-LOGICAL-c498t-9dd472ad5f5cfe50171126d782a061fbe572775c8171ef64fe2475327f255da13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-014-3101-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-014-3101-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24420864$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Martins, Ivone M</creatorcontrib><creatorcontrib>Martins, Fátima</creatorcontrib><creatorcontrib>Belo, Hélio</creatorcontrib><creatorcontrib>Vaz, Madalena</creatorcontrib><creatorcontrib>Carvalho, Marisa</creatorcontrib><creatorcontrib>Cravador, Alfredo</creatorcontrib><creatorcontrib>Choupina, Altino</creatorcontrib><title>Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>Oomycetes from the genus Phytophthora are fungus-like plant pathogens that are devastating for agriculture and natural ecosystems. They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One of the most widely distributed and aggressive Phytophthora species, with more than 1,000 host plants is P. cinnamomi. In this work we report the sequencing and characterization of a class of GIPs secreted by Phytophthora cinnamomi. The gip gene from P. cinnamomi has a 937 bp ORF encoding a putative peptide of 312 deduced amino acids. The expression of this gene was studied during growth in different carbon sources (glucose, cellulose and sawdust), by RT-qPCR and its level of expression was evaluated at five time points. The highest expression of gip gene occurred in sawdust at 8 h of induction. In vivo infection of C. sativa revealed an increase in gip expression from 12 to 24 h. At 36 h its expression decreased suggesting that a compensatory mechanism must occur in plant.</description><subject>Amino Acid Sequence</subject><subject>amino acids</subject><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cannabis - genetics</subject><subject>carbon</subject><subject>cellulose</subject><subject>Cloning, Molecular</subject><subject>ecosystems</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Gene Expression</subject><subject>genes</subject><subject>glucose</subject><subject>Histology</subject><subject>host plants</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Morphology</subject><subject>Oomycetes</subject><subject>open reading frames</subject><subject>Pathogens</subject><subject>Phenotype</subject><subject>Phytophthora</subject><subject>Phytophthora - genetics</subject><subject>Phytophthora cinnamomi</subject><subject>Plant diseases</subject><subject>Plant Diseases - microbiology</subject><subject>plant pathogens</subject><subject>Plant Roots - microbiology</subject><subject>Polymerase chain reaction</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>sawdust</subject><subject>Time Factors</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</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>eNqNkU1rFTEYhYMo9lr9AW50wE0LjubNx2RmKRf7AYUWtOuQO5PcSZlJxiRTrCt_uhmmLeJCugrJ-5yT83IQegv4E2AsPkcATGmJgZUUMJTwDG2AC1qyRtTP0QbT_MhqDgfoVYw3GGMGgr9EB4QxguuKbdDv7eCddfuPRduroNqkg_2lkvWuUK4rrCtubQr-4TINyiVV6J9T0DEulDeFKvbD3Cqnos5Mb3c2-VBMwSedJUen51fHC3bV3yU_9an3QRWtdU6NfrSv0Qujhqjf3J-H6Prk6_ftWXlxeXq-_XJRtqypU9l0HRNEddzw1miOQQCQqhM1UbgCs9NcECF4W-eBNhUzmjDBKRGGcN4poIfoaPXNuX7MOiY52tjqIS-k_RwlcIKpqERTPQEFoA2hwDL64R_0xs_B5UUWCguWQ5NMwUq1wccYtJFTsKMKdxKwXJqUa5MyNymXJuWS992987wbdfeoeKguA2QFYh65vQ5_ff0f1_eryCgv1T7YKK-_kQxgnIFKAP0DksWw9g</recordid><startdate>2014</startdate><enddate>2014</enddate><creator>Martins, Ivone M</creator><creator>Martins, Fátima</creator><creator>Belo, Hélio</creator><creator>Vaz, Madalena</creator><creator>Carvalho, Marisa</creator><creator>Cravador, Alfredo</creator><creator>Choupina, Altino</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</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>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>M7N</scope></search><sort><creationdate>2014</creationdate><title>Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi</title><author>Martins, Ivone M ; Martins, Fátima ; Belo, Hélio ; Vaz, Madalena ; Carvalho, Marisa ; Cravador, Alfredo ; Choupina, Altino</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-9dd472ad5f5cfe50171126d782a061fbe572775c8171ef64fe2475327f255da13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>amino acids</topic><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cannabis - genetics</topic><topic>carbon</topic><topic>cellulose</topic><topic>Cloning, Molecular</topic><topic>ecosystems</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Gene Expression</topic><topic>genes</topic><topic>glucose</topic><topic>Histology</topic><topic>host plants</topic><topic>Life Sciences</topic><topic>Models, Molecular</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Morphology</topic><topic>Oomycetes</topic><topic>open reading frames</topic><topic>Pathogens</topic><topic>Phenotype</topic><topic>Phytophthora</topic><topic>Phytophthora - genetics</topic><topic>Phytophthora cinnamomi</topic><topic>Plant diseases</topic><topic>Plant Diseases - microbiology</topic><topic>plant pathogens</topic><topic>Plant Roots - microbiology</topic><topic>Polymerase chain reaction</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>sawdust</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Martins, Ivone M</creatorcontrib><creatorcontrib>Martins, Fátima</creatorcontrib><creatorcontrib>Belo, Hélio</creatorcontrib><creatorcontrib>Vaz, Madalena</creatorcontrib><creatorcontrib>Carvalho, Marisa</creatorcontrib><creatorcontrib>Cravador, Alfredo</creatorcontrib><creatorcontrib>Choupina, Altino</creatorcontrib><collection>AGRIS</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>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>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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>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>Science 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>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Martins, Ivone M</au><au>Martins, Fátima</au><au>Belo, Hélio</au><au>Vaz, Madalena</au><au>Carvalho, Marisa</au><au>Cravador, Alfredo</au><au>Choupina, Altino</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2014</date><risdate>2014</risdate><volume>41</volume><issue>4</issue><spage>2453</spage><epage>2462</epage><pages>2453-2462</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>Oomycetes from the genus Phytophthora are fungus-like plant pathogens that are devastating for agriculture and natural ecosystems. They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One of the most widely distributed and aggressive Phytophthora species, with more than 1,000 host plants is P. cinnamomi. In this work we report the sequencing and characterization of a class of GIPs secreted by Phytophthora cinnamomi. The gip gene from P. cinnamomi has a 937 bp ORF encoding a putative peptide of 312 deduced amino acids. The expression of this gene was studied during growth in different carbon sources (glucose, cellulose and sawdust), by RT-qPCR and its level of expression was evaluated at five time points. The highest expression of gip gene occurred in sawdust at 8 h of induction. In vivo infection of C. sativa revealed an increase in gip expression from 12 to 24 h. At 36 h its expression decreased suggesting that a compensatory mechanism must occur in plant.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>24420864</pmid><doi>10.1007/s11033-014-3101-1</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence amino acids Animal Anatomy Animal Biochemistry Biomedical and Life Sciences Cannabis - genetics carbon cellulose Cloning, Molecular ecosystems Fungal Proteins - chemistry Fungal Proteins - genetics Gene Expression genes glucose Histology host plants Life Sciences Models, Molecular Molecular biology Molecular Sequence Data Morphology Oomycetes open reading frames Pathogens Phenotype Phytophthora Phytophthora - genetics Phytophthora cinnamomi Plant diseases Plant Diseases - microbiology plant pathogens Plant Roots - microbiology Polymerase chain reaction Protein Conformation Proteins sawdust Time Factors |
| title | Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi |
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