Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan.
Identifieur interne : 000369 ( Main/Exploration ); précédent : 000368; suivant : 000370Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan.
Auteurs : Bing Liu [Suède] ; Sumitha Krishnaswamyreddy [Suède] ; Madhu Nair Muraleedharan [Suède] ; Ke Olson [Suède] ; Anders Broberg [Suède] ; Jerry St Hlberg [Suède] ; Mats Sandgren [Suède]Source :
- PloS one [ 1932-6203 ] ; 2018.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Cellulose (composition chimique), Cellulose (métabolisme), Mannanes (composition chimique), Mannanes (métabolisme), Mixed function oxygenases (composition chimique), Mixed function oxygenases (métabolisme), Modèles moléculaires (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme).
- MESH :
- composition chimique : Cellulose, Mannanes, Mixed function oxygenases, Protéines fongiques.
- enzymologie : Basidiomycota.
- métabolisme : Cellulose, Mannanes, Mixed function oxygenases, Protéines fongiques.
- Modèles moléculaires.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cellulose, Fungal Proteins, Mannans, Mixed Function Oxygenases.
- enzymology : Basidiomycota.
- chemical , metabolism : Cellulose, Fungal Proteins, Mannans, Mixed Function Oxygenases.
- Models, Molecular.
Abstract
Our comparative studies reveal that the two lytic polysaccharide monooxygenases HiLPMO9B and HiLPMO9I from the white-rot conifer pathogen Heterobasidion irregulare display clear difference with respect to their activity against crystalline cellulose and glucomannan. HiLPMO9I produced very little soluble sugar on bacterial microcrystalline cellulose (BMCC). In contrast, HiLPMO9B was much more active against BMCC and even released more soluble sugar than the H. irregulare cellobiohydrolase I, HiCel7A. Furthermore, HiLPMO9B was shown to cooperate with and stimulate the activity of HiCel7A, both when the BMCC was first pretreated with HiLPMO9B, as well as when HiLPMO9B and HiCel7A were added together. No such stimulation was shown by HiLPMO9I. On the other hand, HiLPMO9I was shown to degrade glucomannan, using a C4-oxidizing mechanism, whereas no oxidative cleavage activity of glucomannan was detected for HiLPMO9B. Structural modeling and comparison with other glucomannan-active LPMOs suggest that conserved sugar-interacting residues on the L2, L3 and LC loops may be essential for glucomannan binding, where 4 out of 7 residues are shared by HiLPMO9I, but only one is found in HiLPMO9B. The difference shown between these two H. irregulare LPMOs may reflect distinct biological roles of these enzymes within deconstruction of different plant cell wall polysaccharides during fungal colonization of softwood.
DOI: 10.1371/journal.pone.0203430
PubMed: 30183773
PubMed Central: PMC6124812
Affiliations:
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glucomannan.</title><author><name sortKey="Liu, Bing" sort="Liu, Bing" uniqKey="Liu B" first="Bing" last="Liu">Bing Liu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Krishnaswamyreddy, Sumitha" sort="Krishnaswamyreddy, Sumitha" uniqKey="Krishnaswamyreddy S" first="Sumitha" last="Krishnaswamyreddy">Sumitha Krishnaswamyreddy</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Muraleedharan, Madhu Nair" sort="Muraleedharan, Madhu Nair" uniqKey="Muraleedharan M" first="Madhu Nair" last="Muraleedharan">Madhu Nair Muraleedharan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå</wicri:regionArea><wicri:noRegion>Luleå</wicri:noRegion></affiliation></author><author><name sortKey="Olson, Ke" sort="Olson, Ke" uniqKey="Olson " first=" Ke" last="Olson"> Ke Olson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Forest Mycology and Plant Pathology, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Forest Mycology and Plant Pathology, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Broberg, Anders" sort="Broberg, Anders" uniqKey="Broberg A" first="Anders" last="Broberg">Anders Broberg</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="St Hlberg, Jerry" sort="St Hlberg, Jerry" uniqKey="St Hlberg J" first="Jerry" last="St Hlberg">Jerry St Hlberg</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Sandgren, Mats" sort="Sandgren, Mats" uniqKey="Sandgren M" first="Mats" last="Sandgren">Mats Sandgren</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala</wicri:regionArea><wicri:noRegion>Uppsala</wicri:noRegion></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Cellulose (chemistry)</term><term>Cellulose (metabolism)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (metabolism)</term><term>Mannans (chemistry)</term><term>Mannans (metabolism)</term><term>Mixed Function Oxygenases (chemistry)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Models, Molecular (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Cellulose (composition chimique)</term><term>Cellulose (métabolisme)</term><term>Mannanes (composition chimique)</term><term>Mannanes (métabolisme)</term><term>Mixed function oxygenases (composition chimique)</term><term>Mixed function oxygenases (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulose</term><term>Fungal Proteins</term><term>Mannans</term><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose</term><term>Mannanes</term><term>Mixed function oxygenases</term><term>Protéines fongiques</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" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulose</term><term>Fungal Proteins</term><term>Mannans</term><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose</term><term>Mannanes</term><term>Mixed function oxygenases</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Our comparative studies reveal that the two lytic polysaccharide monooxygenases HiLPMO9B and HiLPMO9I from the white-rot conifer pathogen Heterobasidion irregulare display clear difference with respect to their activity against crystalline cellulose and glucomannan. HiLPMO9I produced very little soluble sugar on bacterial microcrystalline cellulose (BMCC). In contrast, HiLPMO9B was much more active against BMCC and even released more soluble sugar than the H. irregulare cellobiohydrolase I, HiCel7A. Furthermore, HiLPMO9B was shown to cooperate with and stimulate the activity of HiCel7A, both when the BMCC was first pretreated with HiLPMO9B, as well as when HiLPMO9B and HiCel7A were added together. No such stimulation was shown by HiLPMO9I. On the other hand, HiLPMO9I was shown to degrade glucomannan, using a C4-oxidizing mechanism, whereas no oxidative cleavage activity of glucomannan was detected for HiLPMO9B. Structural modeling and comparison with other glucomannan-active LPMOs suggest that conserved sugar-interacting residues on the L2, L3 and LC loops may be essential for glucomannan binding, where 4 out of 7 residues are shared by HiLPMO9I, but only one is found in HiLPMO9B. The difference shown between these two H. irregulare LPMOs may reflect distinct biological roles of these enzymes within deconstruction of different plant cell wall polysaccharides during fungal colonization of softwood.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30183773</PMID><DateCompleted><Year>2019</Year><Month>02</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>03</Month><Day>20</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>13</Volume><Issue>9</Issue><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan.</ArticleTitle><Pagination><MedlinePgn>e0203430</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0203430</ELocationID><Abstract><AbstractText>Our comparative studies reveal that the two lytic polysaccharide monooxygenases HiLPMO9B and HiLPMO9I from the white-rot conifer pathogen Heterobasidion irregulare display clear difference with respect to their activity against crystalline cellulose and glucomannan. HiLPMO9I produced very little soluble sugar on bacterial microcrystalline cellulose (BMCC). In contrast, HiLPMO9B was much more active against BMCC and even released more soluble sugar than the H. irregulare cellobiohydrolase I, HiCel7A. Furthermore, HiLPMO9B was shown to cooperate with and stimulate the activity of HiCel7A, both when the BMCC was first pretreated with HiLPMO9B, as well as when HiLPMO9B and HiCel7A were added together. No such stimulation was shown by HiLPMO9I. On the other hand, HiLPMO9I was shown to degrade glucomannan, using a C4-oxidizing mechanism, whereas no oxidative cleavage activity of glucomannan was detected for HiLPMO9B. Structural modeling and comparison with other glucomannan-active LPMOs suggest that conserved sugar-interacting residues on the L2, L3 and LC loops may be essential for glucomannan binding, where 4 out of 7 residues are shared by HiLPMO9I, but only one is found in HiLPMO9B. The difference shown between these two H. irregulare LPMOs may reflect distinct biological roles of these enzymes within deconstruction of different plant cell wall polysaccharides during fungal colonization of softwood.</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>Krishnaswamyreddy</LastName><ForeName>Sumitha</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muraleedharan</LastName><ForeName>Madhu Nair</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, 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>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>Ståhlberg</LastName><ForeName>Jerry</ForeName><Initials>J</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">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><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>05</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><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008351">Mannans</NameOfSubstance></Chemical><Chemical><RegistryNumber>36W3E5TAMG</RegistryNumber><NameOfSubstance UI="C022901">(1-6)-alpha-glucomannan</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008351" MajorTopicYN="N">Mannans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></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>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>08</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>9</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>9</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>3</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30183773</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0203430</ArticleId><ArticleId IdType="pii">PONE-D-18-20240</ArticleId><ArticleId IdType="pmc">PMC6124812</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Mol Plant Pathol. 2005 Jul 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Madhu Nair" uniqKey="Muraleedharan M" first="Madhu Nair" last="Muraleedharan">Madhu Nair Muraleedharan</name><name sortKey="Olson, Ke" sort="Olson, Ke" uniqKey="Olson " first=" Ke" last="Olson"> Ke Olson</name><name sortKey="Sandgren, Mats" sort="Sandgren, Mats" uniqKey="Sandgren M" first="Mats" last="Sandgren">Mats Sandgren</name><name sortKey="St Hlberg, Jerry" sort="St Hlberg, Jerry" uniqKey="St Hlberg J" first="Jerry" last="St Hlberg">Jerry St Hlberg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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