Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae
The rice blast fungus Magnaporthe oryzae differentiates a specialized infection structure called an appressorium to invade rice cells. In this report, we show that CBP1 , which encodes a chitin-deacetylase, is involved in the induction phase of appressorium differentiation. We demonstrate that the e...
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| Veröffentlicht in: | Scientific reports 2017-08, Vol.7 (1), p.9697-8, Article 9697 |
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| creator | Kuroki, Misa Okauchi, Kana Yoshida, Sho Ohno, Yuko Murata, Sayaka Nakajima, Yuichi Nozaka, Akihito Tanaka, Nobukiyo Nakajima, Masahiro Taguchi, Hayao Saitoh, Ken-ichiro Teraoka, Tohru Narukawa, Megumi Kamakura, Takashi |
| description | The rice blast fungus
Magnaporthe oryzae
differentiates a specialized infection structure called an appressorium to invade rice cells. In this report, we show that
CBP1
, which encodes a chitin-deacetylase, is involved in the induction phase of appressorium differentiation. We demonstrate that the enzymatic activity of Cbp1 is critical for appressorium formation.
M. oryzae
has six CDA homologues in addition to Cbp1, but none of these are indispensable for appressorium formation. We observed chitosan localization at the fungal cell wall using OGA
488
. This observation suggests that Cbp1-catalysed conversion of chitin into chitosan occurs at the cell wall of germ tubes during appressorium differentiation by
M. oryzae
. Taken together, our results provide evidence that the chitin deacetylase activity of Cbp1 is necessary for appressorium formation. |
| doi_str_mv | 10.1038/s41598-017-10322-0 |
| format | Article |
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Magnaporthe oryzae
differentiates a specialized infection structure called an appressorium to invade rice cells. In this report, we show that
CBP1
, which encodes a chitin-deacetylase, is involved in the induction phase of appressorium differentiation. We demonstrate that the enzymatic activity of Cbp1 is critical for appressorium formation.
M. oryzae
has six CDA homologues in addition to Cbp1, but none of these are indispensable for appressorium formation. We observed chitosan localization at the fungal cell wall using OGA
488
. This observation suggests that Cbp1-catalysed conversion of chitin into chitosan occurs at the cell wall of germ tubes during appressorium differentiation by
M. oryzae
. Taken together, our results provide evidence that the chitin deacetylase activity of Cbp1 is necessary for appressorium formation.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-10322-0</identifier><identifier>PMID: 28852173</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14 ; 14/19 ; 14/34 ; 38 ; 631/208/199 ; 631/326/421 ; 82 ; 82/80 ; Amidohydrolases - chemistry ; Amidohydrolases - genetics ; Amidohydrolases - metabolism ; Amino Acid Sequence ; Cell walls ; Chitin ; Chitin - metabolism ; Chitin deacetylase ; Chitosan ; Enzymatic activity ; Enzyme Activation ; Fungi ; Genes ; Genetic Complementation Test ; Germ tubes ; Host-Pathogen Interactions ; Humanities and Social Sciences ; Hydrophobic surfaces ; Infections ; Kinases ; Localization ; Magnaporthe - enzymology ; Magnaporthe - metabolism ; Magnaporthe oryzae ; multidisciplinary ; Mutation ; Oryza ; Oryza - microbiology ; Plant Diseases - microbiology ; Proteins ; Rice ; Rice blast ; Science ; Science (multidisciplinary) ; Signal transduction</subject><ispartof>Scientific reports, 2017-08, Vol.7 (1), p.9697-8, Article 9697</ispartof><rights>The Author(s) 2017</rights><rights>2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-f1d81ca07e7b15ace3755acd7df668a646d29a5d8c8b27ee1e9dbe4d4b617ac13</citedby><cites>FETCH-LOGICAL-c540t-f1d81ca07e7b15ace3755acd7df668a646d29a5d8c8b27ee1e9dbe4d4b617ac13</cites><orcidid>0000-0002-1640-2595</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5575296/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5575296/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,27905,27906,41101,42170,51557,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28852173$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuroki, Misa</creatorcontrib><creatorcontrib>Okauchi, Kana</creatorcontrib><creatorcontrib>Yoshida, Sho</creatorcontrib><creatorcontrib>Ohno, Yuko</creatorcontrib><creatorcontrib>Murata, Sayaka</creatorcontrib><creatorcontrib>Nakajima, Yuichi</creatorcontrib><creatorcontrib>Nozaka, Akihito</creatorcontrib><creatorcontrib>Tanaka, Nobukiyo</creatorcontrib><creatorcontrib>Nakajima, Masahiro</creatorcontrib><creatorcontrib>Taguchi, Hayao</creatorcontrib><creatorcontrib>Saitoh, Ken-ichiro</creatorcontrib><creatorcontrib>Teraoka, Tohru</creatorcontrib><creatorcontrib>Narukawa, Megumi</creatorcontrib><creatorcontrib>Kamakura, Takashi</creatorcontrib><title>Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>The rice blast fungus
Magnaporthe oryzae
differentiates a specialized infection structure called an appressorium to invade rice cells. In this report, we show that
CBP1
, which encodes a chitin-deacetylase, is involved in the induction phase of appressorium differentiation. We demonstrate that the enzymatic activity of Cbp1 is critical for appressorium formation.
M. oryzae
has six CDA homologues in addition to Cbp1, but none of these are indispensable for appressorium formation. We observed chitosan localization at the fungal cell wall using OGA
488
. This observation suggests that Cbp1-catalysed conversion of chitin into chitosan occurs at the cell wall of germ tubes during appressorium differentiation by
M. oryzae
. Taken together, our results provide evidence that the chitin deacetylase activity of Cbp1 is necessary for appressorium formation.</description><subject>14</subject><subject>14/19</subject><subject>14/34</subject><subject>38</subject><subject>631/208/199</subject><subject>631/326/421</subject><subject>82</subject><subject>82/80</subject><subject>Amidohydrolases - chemistry</subject><subject>Amidohydrolases - genetics</subject><subject>Amidohydrolases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Cell walls</subject><subject>Chitin</subject><subject>Chitin - metabolism</subject><subject>Chitin deacetylase</subject><subject>Chitosan</subject><subject>Enzymatic activity</subject><subject>Enzyme Activation</subject><subject>Fungi</subject><subject>Genes</subject><subject>Genetic Complementation Test</subject><subject>Germ tubes</subject><subject>Host-Pathogen Interactions</subject><subject>Humanities and Social Sciences</subject><subject>Hydrophobic surfaces</subject><subject>Infections</subject><subject>Kinases</subject><subject>Localization</subject><subject>Magnaporthe - enzymology</subject><subject>Magnaporthe - metabolism</subject><subject>Magnaporthe oryzae</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>Oryza</subject><subject>Oryza - microbiology</subject><subject>Plant Diseases - microbiology</subject><subject>Proteins</subject><subject>Rice</subject><subject>Rice blast</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Signal transduction</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNp1kU1v1DAQhiMEolXpH-CALHHhkmI7cWxfkNCKj0pFXOBsOfZk11XWDrZTafn1TNlSLUj4Mh7NM69n_DbNS0avGO3U29IzoVVLmWwx57ylT5pzTnvRcsyentzPmstSbikewXXP9PPmjCslOJPdeTNvdqGG2HqwDuphtgWIdTXchXogIfrVQSF2WTKUknJY98SHaYIMsQZbQ4oIkboDkoMDMmJ_JdMat2shX-w22iXl-2rKh58WXjTPJjsXuHyIF833jx--bT63N18_XW_e37RO9LS2E_OKOUslyJEJnKuTAoOXfhoGZYd-8Fxb4ZVTI5cADLQfoff9ODBpHesumndH3WUd9-AdDpvtbJYc9jYfTLLB_F2JYWe26c4IIfGPBhR48yCQ048VSjX7UBzMs42Q1mKY7jrdcy05oq__QW_TmiOuh5SQamBMa6T4kXI5lZJhehyGUXPvpzn6adBP89tPQ7Hp1ekajy1_3EOgOwIFS3EL-eTt_8v-Aq-ErxE</recordid><startdate>20170829</startdate><enddate>20170829</enddate><creator>Kuroki, Misa</creator><creator>Okauchi, Kana</creator><creator>Yoshida, Sho</creator><creator>Ohno, Yuko</creator><creator>Murata, Sayaka</creator><creator>Nakajima, Yuichi</creator><creator>Nozaka, Akihito</creator><creator>Tanaka, Nobukiyo</creator><creator>Nakajima, Masahiro</creator><creator>Taguchi, Hayao</creator><creator>Saitoh, Ken-ichiro</creator><creator>Teraoka, Tohru</creator><creator>Narukawa, Megumi</creator><creator>Kamakura, Takashi</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</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>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1640-2595</orcidid></search><sort><creationdate>20170829</creationdate><title>Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae</title><author>Kuroki, Misa ; Okauchi, Kana ; Yoshida, Sho ; Ohno, Yuko ; Murata, Sayaka ; Nakajima, Yuichi ; Nozaka, Akihito ; Tanaka, Nobukiyo ; Nakajima, Masahiro ; Taguchi, Hayao ; Saitoh, Ken-ichiro ; Teraoka, Tohru ; Narukawa, Megumi ; Kamakura, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-f1d81ca07e7b15ace3755acd7df668a646d29a5d8c8b27ee1e9dbe4d4b617ac13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>14</topic><topic>14/19</topic><topic>14/34</topic><topic>38</topic><topic>631/208/199</topic><topic>631/326/421</topic><topic>82</topic><topic>82/80</topic><topic>Amidohydrolases - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kuroki, Misa</au><au>Okauchi, Kana</au><au>Yoshida, Sho</au><au>Ohno, Yuko</au><au>Murata, Sayaka</au><au>Nakajima, Yuichi</au><au>Nozaka, Akihito</au><au>Tanaka, Nobukiyo</au><au>Nakajima, Masahiro</au><au>Taguchi, Hayao</au><au>Saitoh, Ken-ichiro</au><au>Teraoka, Tohru</au><au>Narukawa, Megumi</au><au>Kamakura, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-08-29</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>9697</spage><epage>8</epage><pages>9697-8</pages><artnum>9697</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>The rice blast fungus
Magnaporthe oryzae
differentiates a specialized infection structure called an appressorium to invade rice cells. In this report, we show that
CBP1
, which encodes a chitin-deacetylase, is involved in the induction phase of appressorium differentiation. We demonstrate that the enzymatic activity of Cbp1 is critical for appressorium formation.
M. oryzae
has six CDA homologues in addition to Cbp1, but none of these are indispensable for appressorium formation. We observed chitosan localization at the fungal cell wall using OGA
488
. This observation suggests that Cbp1-catalysed conversion of chitin into chitosan occurs at the cell wall of germ tubes during appressorium differentiation by
M. oryzae
. Taken together, our results provide evidence that the chitin deacetylase activity of Cbp1 is necessary for appressorium formation.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28852173</pmid><doi>10.1038/s41598-017-10322-0</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-1640-2595</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 14 14/19 14/34 38 631/208/199 631/326/421 82 82/80 Amidohydrolases - chemistry Amidohydrolases - genetics Amidohydrolases - metabolism Amino Acid Sequence Cell walls Chitin Chitin - metabolism Chitin deacetylase Chitosan Enzymatic activity Enzyme Activation Fungi Genes Genetic Complementation Test Germ tubes Host-Pathogen Interactions Humanities and Social Sciences Hydrophobic surfaces Infections Kinases Localization Magnaporthe - enzymology Magnaporthe - metabolism Magnaporthe oryzae multidisciplinary Mutation Oryza Oryza - microbiology Plant Diseases - microbiology Proteins Rice Rice blast Science Science (multidisciplinary) Signal transduction |
| title | Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae |
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