PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: substrate-dependent differential expression within gene families.
Identifieur interne : 000D05 ( Main/Corpus ); précédent : 000D04; suivant : 000D06PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: substrate-dependent differential expression within gene families.
Auteurs : P. Broda ; P R Birch ; P R Brooks ; P F SimsSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1995.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Cellulase (genetics), Cellulase (metabolism), Fungi (enzymology), Fungi (genetics), Gene Expression Regulation, Enzymologic (MeSH), Molecular Sequence Data (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Polymerase Chain Reaction (MeSH), RNA, Messenger (analysis), Substrate Specificity (MeSH), Transcription, Genetic (MeSH).
- MESH :
- chemical , analysis : RNA, Messenger.
- chemical , genetics : Cellulase, Peroxidases.
- chemical , metabolism : Cellulase, Peroxidases.
- enzymology : Fungi.
- genetics : Fungi.
- Base Sequence, Gene Expression Regulation, Enzymologic, Molecular Sequence Data, Polymerase Chain Reaction, Substrate Specificity, Transcription, Genetic.
Abstract
We compare the kinetics of appearance of supernatant enzyme activities (lignin peroxidase, manganese peroxidase, and cellulase) and gene expression (LIG, mnp, and cbhI gene families and the unique cbhII gene) in Phanerochaete chrysosporium ME446 when grown on four different carbon sources: ball-milled straw, representing the natural substrate lignocellulose; Avicel as a crystalline cellulose; and high and low concentrations of glucose, in all cases with limiting nitrogen. PCR-based technology utilizing pairs of primers specific for particular genes showed that there is differential expression between and within the families. There were a number of instances of mRNA species being present only on a single day, implying tight regulation of lignocellulose degradation at the mRNA level. The patterns of extracellular enzyme activities and mnp and cbh gene expression are similar whereas LIG gene expression can be detected when no corresponding enzyme activity is observed in the extracellular supernatant. The enzyme produced under these conditions is presumably sequestered by the mycelium and is likely to be functionally significant. Another striking result is that cellulose, in the form of Avicel, elicits the expression of three LIG gene for which there is no expression under the same conditions with the other carbon sources.
DOI: 10.1128/AEM.61.6.2358-2364.1995
PubMed: 7793956
PubMed Central: PMC167507
Links to Exploration step
pubmed:7793956Le document en format XML
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Broda</name><affiliation><nlm:affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Birch, P R" sort="Birch, P R" uniqKey="Birch P" first="P R" last="Birch">P R Birch</name></author><author><name sortKey="Brooks, P R" sort="Brooks, P R" uniqKey="Brooks P" first="P R" last="Brooks">P R Brooks</name></author><author><name sortKey="Sims, P F" sort="Sims, P F" uniqKey="Sims P" first="P F" last="Sims">P F Sims</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7793956</idno><idno type="pmid">7793956</idno><idno type="pmc">PMC167507</idno><idno type="doi">10.1128/AEM.61.6.2358-2364.1995</idno><idno type="wicri:Area/Main/Corpus">000D05</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D05</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: substrate-dependent differential expression within gene families.</title><author><name sortKey="Broda, P" sort="Broda, P" uniqKey="Broda P" first="P" last="Broda">P. Broda</name><affiliation><nlm:affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Birch, P R" sort="Birch, P R" uniqKey="Birch P" first="P R" last="Birch">P R Birch</name></author><author><name sortKey="Brooks, P R" sort="Brooks, P R" uniqKey="Brooks P" first="P R" last="Brooks">P R Brooks</name></author><author><name sortKey="Sims, P F" sort="Sims, P F" uniqKey="Sims P" first="P F" last="Sims">P F Sims</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="ISSN">0099-2240</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Cellulase (genetics)</term><term>Cellulase (metabolism)</term><term>Fungi (enzymology)</term><term>Fungi (genetics)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Polymerase Chain Reaction (MeSH)</term><term>RNA, Messenger (analysis)</term><term>Substrate Specificity (MeSH)</term><term>Transcription, Genetic (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cellulase</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Gene Expression Regulation, Enzymologic</term><term>Molecular Sequence Data</term><term>Polymerase Chain Reaction</term><term>Substrate Specificity</term><term>Transcription, Genetic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We compare the kinetics of appearance of supernatant enzyme activities (lignin peroxidase, manganese peroxidase, and cellulase) and gene expression (LIG, mnp, and cbhI gene families and the unique cbhII gene) in Phanerochaete chrysosporium ME446 when grown on four different carbon sources: ball-milled straw, representing the natural substrate lignocellulose; Avicel as a crystalline cellulose; and high and low concentrations of glucose, in all cases with limiting nitrogen. PCR-based technology utilizing pairs of primers specific for particular genes showed that there is differential expression between and within the families. There were a number of instances of mRNA species being present only on a single day, implying tight regulation of lignocellulose degradation at the mRNA level. The patterns of extracellular enzyme activities and mnp and cbh gene expression are similar whereas LIG gene expression can be detected when no corresponding enzyme activity is observed in the extracellular supernatant. The enzyme produced under these conditions is presumably sequestered by the mycelium and is likely to be functionally significant. Another striking result is that cellulose, in the form of Avicel, elicits the expression of three LIG gene for which there is no expression under the same conditions with the other carbon sources.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7793956</PMID><DateCompleted><Year>1995</Year><Month>07</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>61</Volume><Issue>6</Issue><PubDate><Year>1995</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: substrate-dependent differential expression within gene families.</ArticleTitle><Pagination><MedlinePgn>2358-64</MedlinePgn></Pagination><Abstract><AbstractText>We compare the kinetics of appearance of supernatant enzyme activities (lignin peroxidase, manganese peroxidase, and cellulase) and gene expression (LIG, mnp, and cbhI gene families and the unique cbhII gene) in Phanerochaete chrysosporium ME446 when grown on four different carbon sources: ball-milled straw, representing the natural substrate lignocellulose; Avicel as a crystalline cellulose; and high and low concentrations of glucose, in all cases with limiting nitrogen. PCR-based technology utilizing pairs of primers specific for particular genes showed that there is differential expression between and within the families. There were a number of instances of mRNA species being present only on a single day, implying tight regulation of lignocellulose degradation at the mRNA level. The patterns of extracellular enzyme activities and mnp and cbh gene expression are similar whereas LIG gene expression can be detected when no corresponding enzyme activity is observed in the extracellular supernatant. The enzyme produced under these conditions is presumably sequestered by the mycelium and is likely to be functionally significant. Another striking result is that cellulose, in the form of Avicel, elicits the expression of three LIG gene for which there is no expression under the same conditions with the other carbon sources.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Broda</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Birch</LastName><ForeName>P R</ForeName><Initials>PR</Initials></Author><Author ValidYN="Y"><LastName>Brooks</LastName><ForeName>P R</ForeName><Initials>PR</Initials></Author><Author ValidYN="Y"><LastName>Sims</LastName><ForeName>P F</ForeName><Initials>PF</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Environ Microbiol</MedlineTA><NlmUniqueID>7605801</NlmUniqueID><ISSNLinking>0099-2240</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>LIG</GeneSymbol><GeneSymbol>cbhI</GeneSymbol><GeneSymbol>cbhII</GeneSymbol><GeneSymbol>mnp</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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