Biochemical studies of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation.
Identifieur interne : 000618 ( Main/Exploration ); précédent : 000617; suivant : 000619Biochemical studies of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation.
Auteurs : Bing Liu [Suède] ; Ke Olson [Suède] ; Miao Wu [Suède] ; Anders Broberg [Suède] ; Mats Sandgren [Suède]Source :
- PloS one [ 1932-6203 ] ; 2017.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Chromatographie d'échange d'ions (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Clustered regularly interspaced short palindromic repeats (MeSH), Lignine (métabolisme), Mixed function oxygenases (composition chimique), Mixed function oxygenases (métabolisme), Pichia (génétique), Polyosides (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Mixed function oxygenases.
- enzymologie : Basidiomycota.
- génétique : Pichia.
- métabolisme : Lignine, Mixed function oxygenases, Polyosides.
- Chromatographie d'échange d'ions, Chromatographie en phase liquide à haute performance, Clustered regularly interspaced short palindromic repeats, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (enzymology), Chromatography, High Pressure Liquid (MeSH), Chromatography, Ion Exchange (MeSH), Clustered Regularly Interspaced Short Palindromic Repeats (MeSH), Lignin (metabolism), Mixed Function Oxygenases (chemistry), Mixed Function Oxygenases (metabolism), Pichia (genetics), Polysaccharides (metabolism), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Mixed Function Oxygenases.
- chemical , metabolism : Lignin, Mixed Function Oxygenases, Polysaccharides.
- enzymology : Basidiomycota.
- genetics : Pichia.
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Clustered Regularly Interspaced Short Palindromic Repeats, Sequence Homology, Amino Acid.
Abstract
Lytic polysaccharide monooxygenases (LPMO) are important redox enzymes produced by microorganisms for the degradation of recalcitrant natural polysaccharides. Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris. The oxidization preferences and substrate specificities of these two enzymes were determined. The two LPMOs were shown to cleave different carbohydrate components of plant cell walls. HiLPMO9H was active on cellulose and oxidized the substrate at the C1 carbon of the pyranose ring at β-1,4-glycosidic linkages, whereas HiLPMO9I cleaved cellulose with strict oxidization at the C4 carbon of glucose unit at internal bonds, and also showed activity against glucomannan. We propose that the two LPMOs play different roles in the plant-cell-wall degrading system of H. irregulare for degradation of softwood and that the lignocellulose degradation mediated by this white-rot fungus may require collective efforts from multi-types of LPMOs.
DOI: 10.1371/journal.pone.0189479
PubMed: 29228039
PubMed Central: PMC5724852
Affiliations:
Links toward previous steps (curation, corpus...)
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Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Chromatographie d'échange d'ions (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Clustered regularly interspaced short palindromic repeats (MeSH)</term><term>Lignine (métabolisme)</term><term>Mixed function oxygenases (composition chimique)</term><term>Mixed function oxygenases (métabolisme)</term><term>Pichia (génétique)</term><term>Polyosides (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Mixed Function Oxygenases</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Mixed function oxygenases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Mixed function oxygenases</term><term>Polyosides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Ion Exchange</term><term>Clustered Regularly Interspaced Short Palindromic Repeats</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term><term>Chromatographie en phase liquide à 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Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris. The oxidization preferences and substrate specificities of these two enzymes were determined. The two LPMOs were shown to cleave different carbohydrate components of plant cell walls. HiLPMO9H was active on cellulose and oxidized the substrate at the C1 carbon of the pyranose ring at β-1,4-glycosidic linkages, whereas HiLPMO9I cleaved cellulose with strict oxidization at the C4 carbon of glucose unit at internal bonds, and also showed activity against glucomannan. We propose that the two LPMOs play different roles in the plant-cell-wall degrading system of H. irregulare for degradation of softwood and that the lignocellulose degradation mediated by this white-rot fungus may require collective efforts from multi-types of LPMOs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29228039</PMID><DateCompleted><Year>2018</Year><Month>01</Month><Day>04</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>12</Issue><PubDate><Year>2017</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Biochemical studies of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation.</ArticleTitle><Pagination><MedlinePgn>e0189479</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0189479</ELocationID><Abstract><AbstractText>Lytic polysaccharide monooxygenases (LPMO) are important redox enzymes produced by microorganisms for the degradation of recalcitrant natural polysaccharides. Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris. The oxidization preferences and substrate specificities of these two enzymes were determined. The two LPMOs were shown to cleave different carbohydrate components of plant cell walls. HiLPMO9H was active on cellulose and oxidized the substrate at the C1 carbon of the pyranose ring at β-1,4-glycosidic linkages, whereas HiLPMO9I cleaved cellulose with strict oxidization at the C4 carbon of glucose unit at internal bonds, and also showed activity against glucomannan. We propose that the two LPMOs play different roles in the plant-cell-wall degrading system of H. irregulare for degradation of softwood and that the lignocellulose degradation mediated by this white-rot fungus may require collective efforts from multi-types of LPMOs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Bing</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Olson</LastName><ForeName>Åke</ForeName><Initials>Å</Initials><AffiliationInfo><Affiliation>Department of Forest Mycology and Plant Pathology, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Miao</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Broberg</LastName><ForeName>Anders</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sandgren</LastName><ForeName>Mats</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2358-4534</Identifier><AffiliationInfo><Affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>12</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United 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MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>10</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>11</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>12</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>12</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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last="Sandgren">Mats Sandgren</name><name sortKey="Wu, Miao" sort="Wu, Miao" uniqKey="Wu M" first="Miao" last="Wu">Miao Wu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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