Improvement of ligninolytic properties by recombinant expression of glyoxal oxidase gene in hyper lignin-degrading fungus Phanerochaete sordida YK-624.
Identifieur interne : 000314 ( Main/Exploration ); précédent : 000313; suivant : 000315Improvement of ligninolytic properties by recombinant expression of glyoxal oxidase gene in hyper lignin-degrading fungus Phanerochaete sordida YK-624.
Auteurs : Yuto Yamada [Japon] ; Jianqiao Wang ; Hirokazu Kawagishi ; Hirofumi HiraiSource :
- Bioscience, biotechnology, and biochemistry [ 1347-6947 ] ; 2014.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Clonage moléculaire (MeSH), Clones cellulaires (MeSH), Expression des gènes (MeSH), Lignine (composition chimique), Lignine (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Plasmides (composition chimique), Plasmides (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Régions promotrices (génétique) (MeSH), Transformation bactérienne (MeSH).
- MESH :
- composition chimique : Lignine, Plasmides.
- enzymologie : Phanerochaete.
- génétique : Alcohol oxidoreductases, Phanerochaete, Protéines fongiques, Protéines recombinantes.
- métabolisme : Alcohol oxidoreductases, Lignine, Plasmides, Protéines fongiques, Protéines recombinantes.
- Clonage moléculaire, Clones cellulaires, Expression des gènes, Régions promotrices (génétique), Transformation bactérienne.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Clone Cells (MeSH), Cloning, Molecular (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Lignin (chemistry), Lignin (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Plasmids (chemistry), Plasmids (metabolism), Promoter Regions, Genetic (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Transformation, Bacterial (MeSH).
- MESH :
- chemical , chemistry : Lignin.
- chemical , genetics : Alcohol Oxidoreductases, Fungal Proteins, Recombinant Proteins.
- chemical , metabolism : Alcohol Oxidoreductases, Fungal Proteins, Lignin, Recombinant Proteins.
- chemistry : Plasmids.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- metabolism : Plasmids.
- Clone Cells, Cloning, Molecular, Gene Expression, Promoter Regions, Genetic, Transformation, Bacterial.
Abstract
Glyoxal oxidase (GLOX) is a source of the extracellular H2O2 required for the oxidation reactions catalyzed by the ligninolytic peroxidases. In the present study, the GLOX-encoding gene (glx) of Phanerochaete chrysosporium was cloned, and bee2 promoter of P. sordida YK-624 was used to drive the expression of glx. The expression plasmid was transformed into a P. sordida YK-624 uracil auxotrophic mutant (strain UV-64), and 16 clones were obtained as GLOX-introducing transformants. These transformants showed higher GLOX activities than wild-type P. sordida YK-624 and control transformants harboring marker plasmid. RT-PCR analysis indicated that the increased GLOX activity was associated with elevated recombinant glx expression. Moreover, these transformants showed higher ligninolytic activity than control transformants. These results suggest that the ligninolytic properties of white-rot fungi can be improved by recombinant expression of glx.
DOI: 10.1080/09168451.2014.946398
PubMed: 25117933
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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uniqKey="Kawagishi H" first="Hirokazu" last="Kawagishi">Hirokazu Kawagishi</name></author><author><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25117933</idno><idno type="pmid">25117933</idno><idno type="doi">10.1080/09168451.2014.946398</idno><idno type="wicri:Area/Main/Corpus">000301</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000301</idno><idno type="wicri:Area/Main/Curation">000301</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000301</idno><idno type="wicri:Area/Main/Exploration">000301</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Improvement of ligninolytic properties by recombinant expression of glyoxal oxidase gene in hyper lignin-degrading fungus Phanerochaete sordida YK-624.</title><author><name sortKey="Yamada, Yuto" sort="Yamada, Yuto" uniqKey="Yamada Y" first="Yuto" last="Yamada">Yuto Yamada</name><affiliation wicri:level="1"><nlm:affiliation>a Department of Applied Biological Chemistry , Graduate School of Agriculture, Shizuoka University , Shizuoka , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>a Department of Applied Biological Chemistry , Graduate School of Agriculture, Shizuoka University , Shizuoka </wicri:regionArea><wicri:noRegion>Shizuoka </wicri:noRegion></affiliation></author><author><name sortKey="Wang, Jianqiao" sort="Wang, Jianqiao" uniqKey="Wang J" first="Jianqiao" last="Wang">Jianqiao Wang</name></author><author><name sortKey="Kawagishi, Hirokazu" sort="Kawagishi, Hirokazu" uniqKey="Kawagishi H" first="Hirokazu" last="Kawagishi">Hirokazu Kawagishi</name></author><author><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name></author></analytic><series><title level="j">Bioscience, biotechnology, and biochemistry</title><idno type="eISSN">1347-6947</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (genetics)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Clone Cells (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Gene Expression (MeSH)</term><term>Lignin (chemistry)</term><term>Lignin (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Plasmids (chemistry)</term><term>Plasmids (metabolism)</term><term>Promoter Regions, Genetic (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Transformation, Bacterial (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (génétique)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Clonage moléculaire (MeSH)</term><term>Clones cellulaires (MeSH)</term><term>Expression des gènes (MeSH)</term><term>Lignine (composition chimique)</term><term>Lignine (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Plasmides (composition chimique)</term><term>Plasmides (métabolisme)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Régions promotrices (génétique) (MeSH)</term><term>Transformation bactérienne (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Fungal Proteins</term><term>Lignin</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plasmids</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lignine</term><term>Plasmides</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Phanerochaete</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plasmids</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Lignine</term><term>Plasmides</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Clone Cells</term><term>Cloning, Molecular</term><term>Gene Expression</term><term>Promoter Regions, Genetic</term><term>Transformation, Bacterial</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Clones cellulaires</term><term>Expression des gènes</term><term>Régions promotrices (génétique)</term><term>Transformation bactérienne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glyoxal oxidase (GLOX) is a source of the extracellular H2O2 required for the oxidation reactions catalyzed by the ligninolytic peroxidases. In the present study, the GLOX-encoding gene (glx) of Phanerochaete chrysosporium was cloned, and bee2 promoter of P. sordida YK-624 was used to drive the expression of glx. The expression plasmid was transformed into a P. sordida YK-624 uracil auxotrophic mutant (strain UV-64), and 16 clones were obtained as GLOX-introducing transformants. These transformants showed higher GLOX activities than wild-type P. sordida YK-624 and control transformants harboring marker plasmid. RT-PCR analysis indicated that the increased GLOX activity was associated with elevated recombinant glx expression. Moreover, these transformants showed higher ligninolytic activity than control transformants. These results suggest that the ligninolytic properties of white-rot fungi can be improved by recombinant expression of glx.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25117933</PMID><DateCompleted><Year>2015</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2014</Year><Month>12</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1347-6947</ISSN><JournalIssue CitedMedium="Internet"><Volume>78</Volume><Issue>12</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Bioscience, biotechnology, and biochemistry</Title><ISOAbbreviation>Biosci Biotechnol Biochem</ISOAbbreviation></Journal><ArticleTitle>Improvement of ligninolytic properties by recombinant expression of glyoxal oxidase gene in hyper lignin-degrading fungus Phanerochaete sordida YK-624.</ArticleTitle><Pagination><MedlinePgn>2128-33</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/09168451.2014.946398</ELocationID><Abstract><AbstractText>Glyoxal oxidase (GLOX) is a source of the extracellular H2O2 required for the oxidation reactions catalyzed by the ligninolytic peroxidases. In the present study, the GLOX-encoding gene (glx) of Phanerochaete chrysosporium was cloned, and bee2 promoter of P. sordida YK-624 was used to drive the expression of glx. The expression plasmid was transformed into a P. sordida YK-624 uracil auxotrophic mutant (strain UV-64), and 16 clones were obtained as GLOX-introducing transformants. These transformants showed higher GLOX activities than wild-type P. sordida YK-624 and control transformants harboring marker plasmid. RT-PCR analysis indicated that the increased GLOX activity was associated with elevated recombinant glx expression. Moreover, these transformants showed higher ligninolytic activity than control transformants. These results suggest that the ligninolytic properties of white-rot fungi can be improved by recombinant expression of glx.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yamada</LastName><ForeName>Yuto</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>a Department of Applied Biological Chemistry , Graduate School of Agriculture, Shizuoka University , Shizuoka , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jianqiao</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kawagishi</LastName><ForeName>Hirokazu</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Hirai</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials></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>2014</Year><Month>08</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biosci Biotechnol Biochem</MedlineTA><NlmUniqueID>9205717</NlmUniqueID><ISSNLinking>0916-8451</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C052371">glyoxal oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002999" MajorTopicYN="N">Clone Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011401" MajorTopicYN="N">Promoter Regions, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014169" MajorTopicYN="N">Transformation, Bacterial</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Phanerochaete sordida YK-624</Keyword><Keyword MajorTopicYN="N">glyoxal oxidase</Keyword><Keyword MajorTopicYN="N">lignin degradation</Keyword><Keyword MajorTopicYN="N">molecular breeding</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>8</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>8</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25117933</ArticleId><ArticleId IdType="doi">10.1080/09168451.2014.946398</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name><name sortKey="Kawagishi, Hirokazu" sort="Kawagishi, Hirokazu" uniqKey="Kawagishi H" first="Hirokazu" last="Kawagishi">Hirokazu Kawagishi</name><name sortKey="Wang, Jianqiao" sort="Wang, Jianqiao" uniqKey="Wang J" first="Jianqiao" last="Wang">Jianqiao Wang</name></noCountry><country name="Japon"><noRegion><name sortKey="Yamada, Yuto" sort="Yamada, Yuto" uniqKey="Yamada Y" first="Yuto" last="Yamada">Yuto Yamada</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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