In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture.
Identifieur interne : 000E17 ( Main/Exploration ); précédent : 000E16; suivant : 000E18In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture.
Auteurs : S M Moukha [France] ; H A Wösten ; M. Asther ; J G WesselsSource :
- Journal of general microbiology [ 0022-1287 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- croissance et développement : Champignons.
- cytologie : Champignons.
- enzymologie : Champignons.
- isolement et purification : Peroxidases.
- métabolisme : Lignine, Peroxidases.
- Immunohistochimie, Manganèse, Techniques microbiologiques.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- cytology : Fungi.
- enzymology : Fungi.
- growth & development : Fungi.
- Immunohistochemistry, Manganese, Microbiological Techniques.
Abstract
Protein secretion and growth were investigated in Phanerochaete chrysosporium by using cultures sandwiched between perforated polycarbonate membranes. Labelling of colonies with radioactive N-acetylglucosamine and L-methionine indicated a close correlation between growth and general protein secretion, even in a central area of the colony secreting the idiophase enzymes lignin peroxidase (LiP) and manganese-dependent lignin peroxidase (MnP). Comparison of the sites of release into the medium of newly synthesized proteins and immuno-detected lignin peroxidases suggested that diffusion of the enzymes from the walls was a limiting step in the release of peroxidases into the medium. Microautoradiography of colonies exposed to N-acetyl[3H]glucosamine revealed the apical growth of thin hyphae and branches (4 to 5 microns diameter on average) in the central secreting area. These secondary hyphae showed peroxidase activity and reacted with lignin peroxidase antibodies. Although it was not possible to directly visualize secretion at hyphal tips, the results suggest that peroxidases (LiP and MnP) are initially secreted at the apex of secondary growing hyphae and later slowly released into the surrounding medium.
DOI: 10.1099/00221287-139-5-969
PubMed: 8336112
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Asther</name></author><author><name sortKey="Wessels, J G" sort="Wessels, J G" uniqKey="Wessels J" first="J G" last="Wessels">J G Wessels</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8336112</idno><idno type="pmid">8336112</idno><idno type="doi">10.1099/00221287-139-5-969</idno><idno type="wicri:Area/Main/Corpus">000E12</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E12</idno><idno type="wicri:Area/Main/Curation">000E12</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E12</idno><idno type="wicri:Area/Main/Exploration">000E12</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture.</title><author><name sortKey="Moukha, S M" sort="Moukha, S M" uniqKey="Moukha S" first="S M" last="Moukha">S M Moukha</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Biotechnologie des Champignons Filamenteux, INRA, Faculté des Sciences de Luminy, Parc Scientifique et Technologique, Marseille, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biotechnologie des Champignons Filamenteux, INRA, Faculté des Sciences de Luminy, Parc Scientifique et Technologique, Marseille</wicri:regionArea><placeName><region type="region">Provence-Alpes-Côte d'Azur</region><region type="old region">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Wosten, H A" sort="Wosten, H A" uniqKey="Wosten H" first="H A" last="Wösten">H A Wösten</name></author><author><name sortKey="Asther, M" sort="Asther, M" uniqKey="Asther M" first="M" last="Asther">M. Asther</name></author><author><name sortKey="Wessels, J G" sort="Wessels, J G" uniqKey="Wessels J" first="J G" last="Wessels">J G Wessels</name></author></analytic><series><title level="j">Journal of general microbiology</title><idno type="ISSN">0022-1287</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fungi (cytology)</term><term>Fungi (enzymology)</term><term>Fungi (growth & development)</term><term>Immunohistochemistry (MeSH)</term><term>Lignin (metabolism)</term><term>Manganese (MeSH)</term><term>Microbiological Techniques (MeSH)</term><term>Peroxidases (isolation & purification)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (croissance et développement)</term><term>Champignons (cytologie)</term><term>Champignons (enzymologie)</term><term>Immunohistochimie (MeSH)</term><term>Lignine (métabolisme)</term><term>Manganèse (MeSH)</term><term>Peroxidases (isolement et purification)</term><term>Peroxidases (métabolisme)</term><term>Techniques microbiologiques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Immunohistochemistry</term><term>Manganese</term><term>Microbiological Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Immunohistochimie</term><term>Manganèse</term><term>Techniques microbiologiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein secretion and growth were investigated in Phanerochaete chrysosporium by using cultures sandwiched between perforated polycarbonate membranes. Labelling of colonies with radioactive N-acetylglucosamine and L-methionine indicated a close correlation between growth and general protein secretion, even in a central area of the colony secreting the idiophase enzymes lignin peroxidase (LiP) and manganese-dependent lignin peroxidase (MnP). Comparison of the sites of release into the medium of newly synthesized proteins and immuno-detected lignin peroxidases suggested that diffusion of the enzymes from the walls was a limiting step in the release of peroxidases into the medium. Microautoradiography of colonies exposed to N-acetyl[3H]glucosamine revealed the apical growth of thin hyphae and branches (4 to 5 microns diameter on average) in the central secreting area. These secondary hyphae showed peroxidase activity and reacted with lignin peroxidase antibodies. Although it was not possible to directly visualize secretion at hyphal tips, the results suggest that peroxidases (LiP and MnP) are initially secreted at the apex of secondary growing hyphae and later slowly released into the surrounding medium.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8336112</PMID><DateCompleted><Year>1993</Year><Month>08</Month><Day>20</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1287</ISSN><JournalIssue CitedMedium="Print"><Volume>139</Volume><Issue>5</Issue><PubDate><Year>1993</Year><Month>May</Month></PubDate></JournalIssue><Title>Journal of general microbiology</Title><ISOAbbreviation>J Gen Microbiol</ISOAbbreviation></Journal><ArticleTitle>In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture.</ArticleTitle><Pagination><MedlinePgn>969-78</MedlinePgn></Pagination><Abstract><AbstractText>Protein secretion and growth were investigated in Phanerochaete chrysosporium by using cultures sandwiched between perforated polycarbonate membranes. Labelling of colonies with radioactive N-acetylglucosamine and L-methionine indicated a close correlation between growth and general protein secretion, even in a central area of the colony secreting the idiophase enzymes lignin peroxidase (LiP) and manganese-dependent lignin peroxidase (MnP). Comparison of the sites of release into the medium of newly synthesized proteins and immuno-detected lignin peroxidases suggested that diffusion of the enzymes from the walls was a limiting step in the release of peroxidases into the medium. Microautoradiography of colonies exposed to N-acetyl[3H]glucosamine revealed the apical growth of thin hyphae and branches (4 to 5 microns diameter on average) in the central secreting area. These secondary hyphae showed peroxidase activity and reacted with lignin peroxidase antibodies. 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Asther</name><name sortKey="Wessels, J G" sort="Wessels, J G" uniqKey="Wessels J" first="J G" last="Wessels">J G Wessels</name><name sortKey="Wosten, H A" sort="Wosten, H A" uniqKey="Wosten H" first="H A" last="Wösten">H A Wösten</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Moukha, S M" sort="Moukha, S M" uniqKey="Moukha S" first="S M" last="Moukha">S M Moukha</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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