Genome and secretome of Chondrostereum purpureum correspond to saprotrophic and phytopathogenic life styles.
Identifieur interne : 000268 ( Main/Exploration ); précédent : 000267; suivant : 000269Genome and secretome of Chondrostereum purpureum correspond to saprotrophic and phytopathogenic life styles.
Auteurs : Rocio Reina [Espagne] ; Harald Kellner [Allemagne] ; Jaqueline Hess [Autriche] ; Nico Jehmlich [Allemagne] ; Immaculada García-Romera [Espagne] ; Elisabet Aranda [Espagne] ; Martin Hofrichter [Allemagne] ; Christiane Liers [Allemagne]Source :
- PloS one [ 1932-6203 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- biosynthèse : Protéines fongiques.
- croissance et développement : Agaricales.
- génétique : Agaricales.
- physiologie : Génome fongique, Régulation de l'expression des gènes fongiques.
English descriptors
- KwdEn :
- MESH :
- chemical , biosynthesis : Fungal Proteins.
- genetics : Agaricales.
- growth & development : Agaricales.
- physiology : Gene Expression Regulation, Fungal, Genome, Fungal.
Abstract
The basidiomycete Chondrostereum purpureum (Silverleaf fungus) is a saprotroph and plant pathogen commercially used for combatting forest "weed" trees in vegetation management. However, little is known about its lignocellulose-degrading capabilities and the enzymatic machinery that is responsible for the degradative potential, and it is not yet clear to which group of wood-rot fungi it actually belongs. Here, we sequenced and analyzed the draft genome of C. purpureum (41.2 Mbp) and performed a quantitative proteomic approach during growth in submerged and solid-state cultures based on soybean meal suspension or containing beech wood supplemented with phenol-rich olive mill residues, respectively. The fungus harbors characteristic lignocellulolytic hydrolases (GH6 and GH7) and oxidoreductases (e.g. laccase, heme peroxidases). High abundance of some of these genes (e.g. 45 laccases, nine GH7) can be explained by gene expansion, e.g. identified for the laccase orthogroup ORTHOMCL11 that exhibits a total of 18 lineage-specific duplications. Other expanded genes families encode for proteins more related to a pathogenic lifestyle (e.g. protease and cytochrome P450s). The fungus responds to the presence of complex growth substrates (lignocellulose, phenolic residues) by the secretion of most of these lignocellulolytic and lignin-modifying enzymes (e.g. alcohol and aryl alcohol oxidases, laccases, GH6, GH7). Based on the genetic and enzymatic constitution, we consider the 'marasmioid' fungus C. purpureum as a 'phytopathogenic' white-rot fungus (WRF) that possesses a complex extracellular enzyme machinery to accomplish efficient lignocellulose degradation during both saprotrophic and phytopathogenic life phases.
DOI: 10.1371/journal.pone.0212769
PubMed: 30822315
PubMed Central: PMC6396904
Affiliations:
- Allemagne, Autriche, Espagne
- District de Leipzig, Saxe (Land), Vienne (Autriche)
- Leipzig, Vienne (Autriche)
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kellner</name><affiliation wicri:level="1"><nlm:affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau</wicri:regionArea><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion></affiliation></author><author><name sortKey="Hess, Jaqueline" sort="Hess, Jaqueline" uniqKey="Hess J" first="Jaqueline" last="Hess">Jaqueline Hess</name><affiliation wicri:level="3"><nlm:affiliation>Department of Botany and Biodiversity Research, University of Vienna, Vienna, Austria.</nlm:affiliation><country xml:lang="fr">Autriche</country><wicri:regionArea>Department of Botany and Biodiversity Research, University of Vienna, Vienna</wicri:regionArea><placeName><settlement 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Científicas, Estación Experimental del Zaidín, Granada</wicri:regionArea><wicri:noRegion>Granada</wicri:noRegion></affiliation></author><author><name sortKey="Hofrichter, Martin" sort="Hofrichter, Martin" uniqKey="Hofrichter M" first="Martin" last="Hofrichter">Martin Hofrichter</name><affiliation wicri:level="1"><nlm:affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau</wicri:regionArea><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion></affiliation></author><author><name sortKey="Liers, Christiane" sort="Liers, Christiane" uniqKey="Liers C" first="Christiane" last="Liers">Christiane Liers</name><affiliation wicri:level="1"><nlm:affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau</wicri:regionArea><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion><wicri:noRegion>Zittau</wicri:noRegion></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (genetics)</term><term>Agaricales (growth & development)</term><term>Fungal Proteins (biosynthesis)</term><term>Gene Expression Regulation, Fungal (physiology)</term><term>Genome, Fungal (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agaricales (croissance et développement)</term><term>Agaricales (génétique)</term><term>Génome fongique (physiologie)</term><term>Protéines fongiques (biosynthèse)</term><term>Régulation de l'expression des gènes fongiques (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Fungal Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Génome fongique</term><term>Régulation de l'expression des gènes fongiques</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Fungal</term><term>Genome, Fungal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The basidiomycete Chondrostereum purpureum (Silverleaf fungus) is a saprotroph and plant pathogen commercially used for combatting forest "weed" trees in vegetation management. However, little is known about its lignocellulose-degrading capabilities and the enzymatic machinery that is responsible for the degradative potential, and it is not yet clear to which group of wood-rot fungi it actually belongs. Here, we sequenced and analyzed the draft genome of C. purpureum (41.2 Mbp) and performed a quantitative proteomic approach during growth in submerged and solid-state cultures based on soybean meal suspension or containing beech wood supplemented with phenol-rich olive mill residues, respectively. The fungus harbors characteristic lignocellulolytic hydrolases (GH6 and GH7) and oxidoreductases (e.g. laccase, heme peroxidases). High abundance of some of these genes (e.g. 45 laccases, nine GH7) can be explained by gene expansion, e.g. identified for the laccase orthogroup ORTHOMCL11 that exhibits a total of 18 lineage-specific duplications. Other expanded genes families encode for proteins more related to a pathogenic lifestyle (e.g. protease and cytochrome P450s). The fungus responds to the presence of complex growth substrates (lignocellulose, phenolic residues) by the secretion of most of these lignocellulolytic and lignin-modifying enzymes (e.g. alcohol and aryl alcohol oxidases, laccases, GH6, GH7). Based on the genetic and enzymatic constitution, we consider the 'marasmioid' fungus C. purpureum as a 'phytopathogenic' white-rot fungus (WRF) that possesses a complex extracellular enzyme machinery to accomplish efficient lignocellulose degradation during both saprotrophic and phytopathogenic life phases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30822315</PMID><DateCompleted><Year>2019</Year><Month>11</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>3</Issue><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Genome and secretome of Chondrostereum purpureum correspond to saprotrophic and phytopathogenic life styles.</ArticleTitle><Pagination><MedlinePgn>e0212769</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0212769</ELocationID><Abstract><AbstractText>The basidiomycete Chondrostereum purpureum (Silverleaf fungus) is a saprotroph and plant pathogen commercially used for combatting forest "weed" trees in vegetation management. However, little is known about its lignocellulose-degrading capabilities and the enzymatic machinery that is responsible for the degradative potential, and it is not yet clear to which group of wood-rot fungi it actually belongs. Here, we sequenced and analyzed the draft genome of C. purpureum (41.2 Mbp) and performed a quantitative proteomic approach during growth in submerged and solid-state cultures based on soybean meal suspension or containing beech wood supplemented with phenol-rich olive mill residues, respectively. The fungus harbors characteristic lignocellulolytic hydrolases (GH6 and GH7) and oxidoreductases (e.g. laccase, heme peroxidases). High abundance of some of these genes (e.g. 45 laccases, nine GH7) can be explained by gene expansion, e.g. identified for the laccase orthogroup ORTHOMCL11 that exhibits a total of 18 lineage-specific duplications. Other expanded genes families encode for proteins more related to a pathogenic lifestyle (e.g. protease and cytochrome P450s). The fungus responds to the presence of complex growth substrates (lignocellulose, phenolic residues) by the secretion of most of these lignocellulolytic and lignin-modifying enzymes (e.g. alcohol and aryl alcohol oxidases, laccases, GH6, GH7). Based on the genetic and enzymatic constitution, we consider the 'marasmioid' fungus C. purpureum as a 'phytopathogenic' white-rot fungus (WRF) that possesses a complex extracellular enzyme machinery to accomplish efficient lignocellulose degradation during both saprotrophic and phytopathogenic life phases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reina</LastName><ForeName>Rocio</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Soil Microbiology and Symbiotic Systems, Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Granada, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kellner</LastName><ForeName>Harald</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hess</LastName><ForeName>Jaqueline</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Botany and Biodiversity Research, University of Vienna, Vienna, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jehmlich</LastName><ForeName>Nico</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Molecular Systems Biology, Helmholtz-Centre for Environmental Research, Leipzig, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>García-Romera</LastName><ForeName>Immaculada</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Soil Microbiology and Symbiotic Systems, Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Granada, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aranda</LastName><ForeName>Elisabet</ForeName><Initials>E</Initials><Identifier Source="ORCID">0000-0001-5915-2445</Identifier><AffiliationInfo><Affiliation>Department of Soil Microbiology and Symbiotic Systems, Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Granada, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hofrichter</LastName><ForeName>Martin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liers</LastName><ForeName>Christiane</ForeName><Initials>C</Initials><Identifier Source="ORCID">0000-0002-2000-0820</Identifier><AffiliationInfo><Affiliation>Unit of Environmental Biotechnology, Dresden University of Technology, International Institute Zittau, Zittau, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>03</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000363" MajorTopicYN="Y">Agaricales</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="Y">Fungal Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016681" MajorTopicYN="N">Genome, Fungal</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><CoiStatement>The authors have declared that no competing interests exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>07</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>02</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>3</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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