N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of ectomycorrhizal fungi: Boletales and Agaricales.
Identifieur interne : 000921 ( Main/Corpus ); précédent : 000920; suivant : 000922N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of ectomycorrhizal fungi: Boletales and Agaricales.
Auteurs : François Maillard ; Margaux Didion ; Laure Fauchery ; Cyrille Bach ; Marc BuéeSource :
- Mycorrhiza [ 1432-1890 ] ; 2018.
English descriptors
- KwdEn :
- Acetylglucosaminidase (genetics), Acetylglucosaminidase (metabolism), Agaricales (enzymology), Agaricales (genetics), Basidiomycota (enzymology), Basidiomycota (genetics), Chitin (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation (MeSH), Mycorrhizae (enzymology), Mycorrhizae (genetics), Species Specificity (MeSH).
- MESH :
- chemical , genetics : Acetylglucosaminidase, Fungal Proteins.
- chemical , metabolism : Acetylglucosaminidase, Chitin, Fungal Proteins.
- enzymology : Agaricales, Basidiomycota, Mycorrhizae.
- genetics : Agaricales, Basidiomycota, Mycorrhizae.
- Gene Expression Regulation, Species Specificity.
Abstract
Chitin is one of the most abundant nitrogen-containing polymers in forest soil. Ability of ectomycorrhizal (EM) fungi to utilize chitin may play a key role in the EM symbiosis nutrition and soil carbon cycle. In forest, EM fungi exhibit high diversity, which could be based on function partitioning and trait complementarity. Although it has long been recognized that closely related species share functional characteristics, the phylogenetic conservatism of functional traits within microorganisms remains unclear. Because extracellular N-acetylglucosaminidase activity has been proposed as functional trait of chitin degradation, we screened this activity on 35 EM fungi species with or without chitin in the growth medium to (i) describe the functional diversity of EM fungi and (ii) identify potential links between this functional trait and EM fungal phylogeny. We observed large variations of the extracellular N-acetylglucosaminidase activities among the fungal strains. Furthermore, our results revealed two regulation patterns of extracellular N-acetylglucosaminidase activities. Indeed, these chitinolytic activities were stimulated or repressed in the presence of chitin, in comparison to the control treatment. These profiles of extracellular N-acetylglucosaminidase stimulation/repression might be conserved at a high phylogenetic level in the Basidiomycota phylum, as illustrated by the opposite patterns of regulation between Boletales and Agaricales. Finally, the downregulation of this activity by chitin, for some EM fungal groups, might suggest another chitin degradation pathway.
DOI: 10.1007/s00572-018-0833-0
PubMed: 29654366
Links to Exploration step
pubmed:29654366Le document en format XML
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France.</nlm:affiliation></affiliation></author><author><name sortKey="Bach, Cyrille" sort="Bach, Cyrille" uniqKey="Bach C" first="Cyrille" last="Bach">Cyrille Bach</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Buee, Marc" sort="Buee, Marc" uniqKey="Buee M" first="Marc" last="Buée">Marc Buée</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France. marc.buee@inra.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29654366</idno><idno type="pmid">29654366</idno><idno type="doi">10.1007/s00572-018-0833-0</idno><idno type="wicri:Area/Main/Corpus">000921</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000921</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of ectomycorrhizal fungi: Boletales and Agaricales.</title><author><name sortKey="Maillard, Francois" sort="Maillard, Francois" uniqKey="Maillard F" first="François" last="Maillard">François Maillard</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Didion, Margaux" sort="Didion, Margaux" uniqKey="Didion M" first="Margaux" last="Didion">Margaux Didion</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Fauchery, Laure" sort="Fauchery, Laure" uniqKey="Fauchery L" first="Laure" last="Fauchery">Laure Fauchery</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Bach, Cyrille" sort="Bach, Cyrille" uniqKey="Bach C" first="Cyrille" last="Bach">Cyrille Bach</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Buee, Marc" sort="Buee, Marc" uniqKey="Buee M" first="Marc" last="Buée">Marc Buée</name><affiliation><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France. marc.buee@inra.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Mycorrhiza</title><idno type="eISSN">1432-1890</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylglucosaminidase (genetics)</term><term>Acetylglucosaminidase (metabolism)</term><term>Agaricales (enzymology)</term><term>Agaricales (genetics)</term><term>Basidiomycota (enzymology)</term><term>Basidiomycota (genetics)</term><term>Chitin (metabolism)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Gene Expression Regulation (MeSH)</term><term>Mycorrhizae (enzymology)</term><term>Mycorrhizae (genetics)</term><term>Species Specificity (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetylglucosaminidase</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetylglucosaminidase</term><term>Chitin</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term><term>Basidiomycota</term><term>Mycorrhizae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Agaricales</term><term>Basidiomycota</term><term>Mycorrhizae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chitin is one of the most abundant nitrogen-containing polymers in forest soil. Ability of ectomycorrhizal (EM) fungi to utilize chitin may play a key role in the EM symbiosis nutrition and soil carbon cycle. In forest, EM fungi exhibit high diversity, which could be based on function partitioning and trait complementarity. Although it has long been recognized that closely related species share functional characteristics, the phylogenetic conservatism of functional traits within microorganisms remains unclear. Because extracellular N-acetylglucosaminidase activity has been proposed as functional trait of chitin degradation, we screened this activity on 35 EM fungi species with or without chitin in the growth medium to (i) describe the functional diversity of EM fungi and (ii) identify potential links between this functional trait and EM fungal phylogeny. We observed large variations of the extracellular N-acetylglucosaminidase activities among the fungal strains. Furthermore, our results revealed two regulation patterns of extracellular N-acetylglucosaminidase activities. Indeed, these chitinolytic activities were stimulated or repressed in the presence of chitin, in comparison to the control treatment. These profiles of extracellular N-acetylglucosaminidase stimulation/repression might be conserved at a high phylogenetic level in the Basidiomycota phylum, as illustrated by the opposite patterns of regulation between Boletales and Agaricales. Finally, the downregulation of this activity by chitin, for some EM fungal groups, might suggest another chitin degradation pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29654366</PMID><DateCompleted><Year>2018</Year><Month>09</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>09</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1890</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>4</Issue><PubDate><Year>2018</Year><Month>May</Month></PubDate></JournalIssue><Title>Mycorrhiza</Title><ISOAbbreviation>Mycorrhiza</ISOAbbreviation></Journal><ArticleTitle>N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of ectomycorrhizal fungi: Boletales and Agaricales.</ArticleTitle><Pagination><MedlinePgn>391-397</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00572-018-0833-0</ELocationID><Abstract><AbstractText>Chitin is one of the most abundant nitrogen-containing polymers in forest soil. Ability of ectomycorrhizal (EM) fungi to utilize chitin may play a key role in the EM symbiosis nutrition and soil carbon cycle. In forest, EM fungi exhibit high diversity, which could be based on function partitioning and trait complementarity. Although it has long been recognized that closely related species share functional characteristics, the phylogenetic conservatism of functional traits within microorganisms remains unclear. Because extracellular N-acetylglucosaminidase activity has been proposed as functional trait of chitin degradation, we screened this activity on 35 EM fungi species with or without chitin in the growth medium to (i) describe the functional diversity of EM fungi and (ii) identify potential links between this functional trait and EM fungal phylogeny. We observed large variations of the extracellular N-acetylglucosaminidase activities among the fungal strains. Furthermore, our results revealed two regulation patterns of extracellular N-acetylglucosaminidase activities. Indeed, these chitinolytic activities were stimulated or repressed in the presence of chitin, in comparison to the control treatment. These profiles of extracellular N-acetylglucosaminidase stimulation/repression might be conserved at a high phylogenetic level in the Basidiomycota phylum, as illustrated by the opposite patterns of regulation between Boletales and Agaricales. Finally, the downregulation of this activity by chitin, for some EM fungal groups, might suggest another chitin degradation pathway.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maillard</LastName><ForeName>François</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Didion</LastName><ForeName>Margaux</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fauchery</LastName><ForeName>Laure</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bach</LastName><ForeName>Cyrille</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Buée</LastName><ForeName>Marc</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-8614-3886</Identifier><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000, Nancy, France. marc.buee@inra.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>04</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Mycorrhiza</MedlineTA><NlmUniqueID>100955036</NlmUniqueID><ISSNLinking>0940-6360</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>1398-61-4</RegistryNumber><NameOfSubstance UI="D002686">Chitin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.52</RegistryNumber><NameOfSubstance UI="D000118">Acetylglucosaminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000118" MajorTopicYN="N">Acetylglucosaminidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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