Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000B00 ( Main/Corpus ); précédent : 000A99; suivant : 000B01Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Laura Zacchi ; Ian Morris ; Patricia J. HarveySource :
- Microbiology (Reading, England) [ 1350-0872 ] ; 2000.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Carbon, Peroxidases.
- chemical : Culture Media.
- enzymology : Phanerochaete.
- growth & development : Phanerochaete.
- ultrastructure : Phanerochaete.
- Microscopy, Electron, Oxidative Stress.
Abstract
The practice of exposing liquid cultures of the white-rot fungus Phanerochaete chrysosporium to a pure oxygen atmosphere under conditions of nutrient starvation has been widely adopted to induce lignin peroxidase (LiP) synthesis. Transmission electron microscopy was used to examine hyphal cells of carbon-limited cultures that had been exposed to an atmosphere of pure oxygen, and revealed evidence of a major loss in organization of cellular ultrastructure, which may be attributed to oxygen toxicity. Under some conditions (continuous agitation in air with cellulose as the carbon source) cultures will produce LiP without needing to be exposed to a pure oxygen atmosphere. A similar major loss of cellular ultrastructure was found in hyphal cells from such cultures upon examination. Investigation of the levels of H2O2, catalase and carbonyl content of intracellular proteins suggests that the latter cultures developed a hyperoxidant state because the rate of supply of carbon from cellulose hydrolysis was insufficient for oxygen homeostasis. The association of LiP with these cultures and with those exposed to an atmosphere of pure oxygen infers that LiP may be triggered in response to oxidant stress.
DOI: 10.1099/00221287-146-3-759
PubMed: 10746780
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pubmed:10746780Le document en format XML
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Harvey</name><affiliation><nlm:affiliation>School of Chemical and Life Sciences, University of Greenwich, Wellington Street, London SE18 6PF, UK1.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10746780</idno><idno type="pmid">10746780</idno><idno type="doi">10.1099/00221287-146-3-759</idno><idno type="wicri:Area/Main/Corpus">000B00</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B00</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium.</title><author><name sortKey="Zacchi, Laura" sort="Zacchi, Laura" uniqKey="Zacchi L" first="Laura" last="Zacchi">Laura Zacchi</name><affiliation><nlm:affiliation>School of Chemical and Life Sciences, University of Greenwich, Wellington Street, London SE18 6PF, UK1.</nlm:affiliation></affiliation></author><author><name sortKey="Morris, Ian" sort="Morris, Ian" uniqKey="Morris I" first="Ian" last="Morris">Ian Morris</name><affiliation><nlm:affiliation>Department of Biology, Imperial College of Science Technology & Medicine, Prince Consort Road, London SW7 2BB, UK2.</nlm:affiliation></affiliation></author><author><name sortKey="Harvey, Patricia J" sort="Harvey, Patricia J" uniqKey="Harvey P" first="Patricia J" last="Harvey">Patricia J. Harvey</name><affiliation><nlm:affiliation>School of Chemical and Life Sciences, University of Greenwich, Wellington Street, London SE18 6PF, UK1.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Microbiology (Reading, England)</title><idno type="ISSN">1350-0872</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbon (metabolism)</term><term>Culture Media (MeSH)</term><term>Microscopy, Electron (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (growth & development)</term><term>Phanerochaete (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbon</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Culture Media</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Microscopy, Electron</term><term>Oxidative Stress</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The practice of exposing liquid cultures of the white-rot fungus Phanerochaete chrysosporium to a pure oxygen atmosphere under conditions of nutrient starvation has been widely adopted to induce lignin peroxidase (LiP) synthesis. Transmission electron microscopy was used to examine hyphal cells of carbon-limited cultures that had been exposed to an atmosphere of pure oxygen, and revealed evidence of a major loss in organization of cellular ultrastructure, which may be attributed to oxygen toxicity. Under some conditions (continuous agitation in air with cellulose as the carbon source) cultures will produce LiP without needing to be exposed to a pure oxygen atmosphere. A similar major loss of cellular ultrastructure was found in hyphal cells from such cultures upon examination. Investigation of the levels of H2O2, catalase and carbonyl content of intracellular proteins suggests that the latter cultures developed a hyperoxidant state because the rate of supply of carbon from cellulose hydrolysis was insufficient for oxygen homeostasis. The association of LiP with these cultures and with those exposed to an atmosphere of pure oxygen infers that LiP may be triggered in response to oxidant stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10746780</PMID><DateCompleted><Year>2000</Year><Month>06</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>08</Month><Day>26</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1350-0872</ISSN><JournalIssue CitedMedium="Print"><Volume>146 ( Pt 3)</Volume><PubDate><Year>2000</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Microbiology (Reading, England)</Title><ISOAbbreviation>Microbiology (Reading)</ISOAbbreviation></Journal><ArticleTitle>Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>759-765</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1099/00221287-146-3-759</ELocationID><Abstract><AbstractText>The practice of exposing liquid cultures of the white-rot fungus Phanerochaete chrysosporium to a pure oxygen atmosphere under conditions of nutrient starvation has been widely adopted to induce lignin peroxidase (LiP) synthesis. Transmission electron microscopy was used to examine hyphal cells of carbon-limited cultures that had been exposed to an atmosphere of pure oxygen, and revealed evidence of a major loss in organization of cellular ultrastructure, which may be attributed to oxygen toxicity. Under some conditions (continuous agitation in air with cellulose as the carbon source) cultures will produce LiP without needing to be exposed to a pure oxygen atmosphere. A similar major loss of cellular ultrastructure was found in hyphal cells from such cultures upon examination. Investigation of the levels of H2O2, catalase and carbonyl content of intracellular proteins suggests that the latter cultures developed a hyperoxidant state because the rate of supply of carbon from cellulose hydrolysis was insufficient for oxygen homeostasis. The association of LiP with these cultures and with those exposed to an atmosphere of pure oxygen infers that LiP may be triggered in response to oxidant stress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zacchi</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>School of Chemical and Life Sciences, University of Greenwich, Wellington Street, London SE18 6PF, UK1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morris</LastName><ForeName>Ian</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Biology, Imperial College of Science Technology & Medicine, Prince Consort Road, London SW7 2BB, UK2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harvey</LastName><ForeName>Patricia J</ForeName><Initials>PJ</Initials><AffiliationInfo><Affiliation>School of Chemical and Life Sciences, University of Greenwich, Wellington Street, London SE18 6PF, UK1.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Microbiology (Reading)</MedlineTA><NlmUniqueID>9430468</NlmUniqueID><ISSNLinking>1350-0872</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-44-0</RegistryNumber><NameOfSubstance UI="D002244">Carbon</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002244" MajorTopicYN="N">Carbon</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>4</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>6</Month><Day>24</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>4</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10746780</ArticleId><ArticleId IdType="doi">10.1099/00221287-146-3-759</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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