Phenotypic classes of phenoloxidase-negative mutants of the lignin-degrading fungus Phanerochaete chrysosporium.
Identifieur interne : 001050 ( Main/Exploration ); précédent : 001049; suivant : 001051Phenotypic classes of phenoloxidase-negative mutants of the lignin-degrading fungus Phanerochaete chrysosporium.
Auteurs : R. Liwicki ; A. Paterson ; M J Macdonald ; P. BrodaSource :
- Journal of bacteriology [ 0021-9193 ] ; 1985.
Descripteurs français
- KwdFr :
- MESH :
- déficit : Monophenol monooxygenase.
- effets des radiations : Champignons.
- génétique : Catechol oxidase, Champignons, Monophenol monooxygenase.
- métabolisme : Champignons, Lignine.
- Phénotype, Rayons gamma.
English descriptors
- KwdEn :
- MESH :
- chemical , deficiency : Monophenol Monooxygenase.
- chemical , genetics : Catechol Oxidase, Monophenol Monooxygenase.
- genetics : Fungi.
- metabolism : Fungi, Lignin.
- radiation effects : Fungi.
- Gamma Rays, Phenotype.
Abstract
This paper reports the isolation of phenoloxidase-negative mutants of the white-rot fungus Phanerochaete chrysosporium and the results of a survey of idiophasic functions among these mutants. The mutant strains were isolated from a medium containing o-anisidine after gamma irradiation of wild-type spores and fell into four classes, divided by the manner in which they mineralized 14C-lignin wheat lignocellulose. Examples are strain LMT7, which degraded lignin at a rate similar to that of the wild type; strain LMT26, in which degradation was enhanced; strain LMT16, whose degradation rate was apparently unaffected, although the onset of lignin attack was delayed compared with that in the wild type; and strain LMT24, which was unable to evolve significant amounts of 14CO2 from the radiolabeled substrate. The mutants were not necessarily defective in other functions associated with idiophasic activities (intracellular cyclic AMP levels, sporulation, extracellular glucan production, veratryl alcohol synthesis). We conclude that phenoloxidase activity as detected by the o-anisidine plate test is not necessary for lignin degradation. In addition, mutations resulting in the loss of lignin-degrading ability were not necessarily pleiotropic with other idiophasic functions.
DOI: 10.1128/JB.162.2.641-644.1985
PubMed: 3921527
PubMed Central: PMC218897
Affiliations:
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Le document en format XML
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The mutant strains were isolated from a medium containing o-anisidine after gamma irradiation of wild-type spores and fell into four classes, divided by the manner in which they mineralized 14C-lignin wheat lignocellulose. Examples are strain LMT7, which degraded lignin at a rate similar to that of the wild type; strain LMT26, in which degradation was enhanced; strain LMT16, whose degradation rate was apparently unaffected, although the onset of lignin attack was delayed compared with that in the wild type; and strain LMT24, which was unable to evolve significant amounts of 14CO2 from the radiolabeled substrate. The mutants were not necessarily defective in other functions associated with idiophasic activities (intracellular cyclic AMP levels, sporulation, extracellular glucan production, veratryl alcohol synthesis). We conclude that phenoloxidase activity as detected by the o-anisidine plate test is not necessary for lignin degradation. In addition, mutations resulting in the loss of lignin-degrading ability were not necessarily pleiotropic with other idiophasic functions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3921527</PMID><DateCompleted><Year>1985</Year><Month>06</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9193</ISSN><JournalIssue CitedMedium="Print"><Volume>162</Volume><Issue>2</Issue><PubDate><Year>1985</Year><Month>May</Month></PubDate></JournalIssue><Title>Journal of bacteriology</Title><ISOAbbreviation>J Bacteriol</ISOAbbreviation></Journal><ArticleTitle>Phenotypic classes of phenoloxidase-negative mutants of the lignin-degrading fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>641-4</MedlinePgn></Pagination><Abstract><AbstractText>This paper reports the isolation of phenoloxidase-negative mutants of the white-rot fungus Phanerochaete chrysosporium and the results of a survey of idiophasic functions among these mutants. The mutant strains were isolated from a medium containing o-anisidine after gamma irradiation of wild-type spores and fell into four classes, divided by the manner in which they mineralized 14C-lignin wheat lignocellulose. Examples are strain LMT7, which degraded lignin at a rate similar to that of the wild type; strain LMT26, in which degradation was enhanced; strain LMT16, whose degradation rate was apparently unaffected, although the onset of lignin attack was delayed compared with that in the wild type; and strain LMT24, which was unable to evolve significant amounts of 14CO2 from the radiolabeled substrate. The mutants were not necessarily defective in other functions associated with idiophasic activities (intracellular cyclic AMP levels, sporulation, extracellular glucan production, veratryl alcohol synthesis). We conclude that phenoloxidase activity as detected by the o-anisidine plate test is not necessary for lignin degradation. In addition, mutations resulting in the loss of lignin-degrading ability were not necessarily pleiotropic with other idiophasic functions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liwicki</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Paterson</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>MacDonald</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Broda</LastName><ForeName>P</ForeName><Initials>P</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>J Bacteriol</MedlineTA><NlmUniqueID>2985120R</NlmUniqueID><ISSNLinking>0021-9193</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.1</RegistryNumber><NameOfSubstance UI="D004156">Catechol Oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.18.1</RegistryNumber><NameOfSubstance UI="D014442">Monophenol Monooxygenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004156" MajorTopicYN="N">Catechol Oxidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000528" MajorTopicYN="N">radiation effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005720" MajorTopicYN="N">Gamma Rays</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014442" MajorTopicYN="N">Monophenol Monooxygenase</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1985</Year><Month>5</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1985</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1985</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3921527</ArticleId><ArticleId IdType="pmc">PMC218897</ArticleId><ArticleId IdType="doi">10.1128/JB.162.2.641-644.1985</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Bacteriol. 1980 Nov;144(2):509-17</Citation><ArticleIdList><ArticleId IdType="pubmed">7000747</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Soc Symp. 1983;48:87-95</Citation><ArticleIdList><ArticleId IdType="pubmed">6400486</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1984 Apr;81(8):2280-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16593451</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1984 Oct;160(1):470-2</Citation><ArticleIdList><ArticleId IdType="pubmed">6090435</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1973 Apr;114(1):7-10</Citation><ArticleIdList><ArticleId IdType="pubmed">4633351</ArticleId></ArticleIdList></Reference><Reference><Citation>Radiat Res. 1973 Jan;53(1):77-87</Citation><ArticleIdList><ArticleId IdType="pubmed">4265447</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Broda, P" sort="Broda, P" uniqKey="Broda P" first="P" last="Broda">P. Broda</name><name sortKey="Liwicki, R" sort="Liwicki, R" uniqKey="Liwicki R" first="R" last="Liwicki">R. Liwicki</name><name sortKey="Macdonald, M J" sort="Macdonald, M J" uniqKey="Macdonald M" first="M J" last="Macdonald">M J Macdonald</name><name sortKey="Paterson, A" sort="Paterson, A" uniqKey="Paterson A" first="A" last="Paterson">A. Paterson</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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