Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium.
Identifieur interne : 000E69 ( Main/Exploration ); précédent : 000E68; suivant : 000E70Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium.
Auteurs : E A Pease [États-Unis] ; M. TienSource :
- Journal of bacteriology [ 0021-9193 ] ; 1992.
Descripteurs français
- KwdFr :
- ARN messager (analyse), Acides aminés (analyse), Champignons (enzymologie), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Isoenzymes (métabolisme), Manganèse (pharmacologie), Milieux de culture (pharmacologie), Peroxidases (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Similitude de séquences d'acides nucléiques (MeSH), Stabilité enzymatique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- analyse : ARN messager, Acides aminés.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques.
- enzymologie : Champignons.
- métabolisme : Isoenzymes, Peroxidases.
- pharmacologie : Manganèse, Milieux de culture.
- Cinétique, Données de séquences moléculaires, Similitude de séquences d'acides nucléiques, Stabilité enzymatique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (analysis), Culture Media (pharmacology), Enzyme Stability (MeSH), Fungi (enzymology), Gene Expression Regulation, Fungal (drug effects), Isoenzymes (metabolism), Kinetics (MeSH), Manganese (pharmacology), Molecular Sequence Data (MeSH), Peroxidases (metabolism), RNA, Messenger (analysis), Sequence Homology, Nucleic Acid (MeSH).
- MESH :
- chemical , analysis : Amino Acids, RNA, Messenger.
- chemical , metabolism : Isoenzymes, Peroxidases.
- chemical , pharmacology : Culture Media, Manganese.
- drug effects : Gene Expression Regulation, Fungal.
- enzymology : Fungi.
- Amino Acid Sequence, Enzyme Stability, Kinetics, Molecular Sequence Data, Sequence Homology, Nucleic Acid.
Abstract
Lignin and Mn peroxidases are two families of isozymes produced by the lignin-degrading fungus Phanerochaete chrysosporium under nutrient nitrogen or carbon limitation. We purified to homogeneity the three major Mn peroxidase isozymes, H3 (pI = 4.9), H4 (pI = 4.5), and H5 (pI = 4.2). Amino-terminal sequencing of these isozymes demonstrates that they are encoded by different genes. We also analyzed the regulation of these isozymes in carbon- and nitrogen-limited cultures and found not only that the lignin and Mn peroxidases are differentially regulated but also that differential regulation occurs within the Mn peroxidase isozyme family. The isozyme profile and the time at which each isozyme appears in secondary metabolism differ in both nitrogen- and carbon-limited cultures. Each isozyme also responded differently to the addition of a putative inducer, divalent Mn. The stability of the Mn peroxidases in carbon- and nitrogen-limited cultures was also characterized after cycloheximide addition. The Mn peroxidases are more stable in carbon-limited cultures than in nitrogen-limited cultures. They are also more stable than the lignin peroxidases. These data collectively suggest that the Mn peroxidase isozymes serve different functions in lignin biodegradation.
DOI: 10.1128/jb.174.11.3532-3540.1992
PubMed: 1592808
PubMed Central: PMC206038
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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We purified to homogeneity the three major Mn peroxidase isozymes, H3 (pI = 4.9), H4 (pI = 4.5), and H5 (pI = 4.2). Amino-terminal sequencing of these isozymes demonstrates that they are encoded by different genes. We also analyzed the regulation of these isozymes in carbon- and nitrogen-limited cultures and found not only that the lignin and Mn peroxidases are differentially regulated but also that differential regulation occurs within the Mn peroxidase isozyme family. The isozyme profile and the time at which each isozyme appears in secondary metabolism differ in both nitrogen- and carbon-limited cultures. Each isozyme also responded differently to the addition of a putative inducer, divalent Mn. The stability of the Mn peroxidases in carbon- and nitrogen-limited cultures was also characterized after cycloheximide addition. The Mn peroxidases are more stable in carbon-limited cultures than in nitrogen-limited cultures. They are also more stable than the lignin peroxidases. These data collectively suggest that the Mn peroxidase isozymes serve different functions in lignin biodegradation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1592808</PMID><DateCompleted><Year>1992</Year><Month>07</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9193</ISSN><JournalIssue CitedMedium="Print"><Volume>174</Volume><Issue>11</Issue><PubDate><Year>1992</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of bacteriology</Title><ISOAbbreviation>J Bacteriol</ISOAbbreviation></Journal><ArticleTitle>Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>3532-40</MedlinePgn></Pagination><Abstract><AbstractText>Lignin and Mn peroxidases are two families of isozymes produced by the lignin-degrading fungus Phanerochaete chrysosporium under nutrient nitrogen or carbon limitation. We purified to homogeneity the three major Mn peroxidase isozymes, H3 (pI = 4.9), H4 (pI = 4.5), and H5 (pI = 4.2). Amino-terminal sequencing of these isozymes demonstrates that they are encoded by different genes. We also analyzed the regulation of these isozymes in carbon- and nitrogen-limited cultures and found not only that the lignin and Mn peroxidases are differentially regulated but also that differential regulation occurs within the Mn peroxidase isozyme family. The isozyme profile and the time at which each isozyme appears in secondary metabolism differ in both nitrogen- and carbon-limited cultures. Each isozyme also responded differently to the addition of a putative inducer, divalent Mn. The stability of the Mn peroxidases in carbon- and nitrogen-limited cultures was also characterized after cycloheximide addition. The Mn peroxidases are more stable in carbon-limited cultures than in nitrogen-limited cultures. They are also more stable than the lignin peroxidases. These data collectively suggest that the Mn peroxidase isozymes serve different functions in lignin biodegradation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pease</LastName><ForeName>E A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1-P42ES04922-01</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType 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UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" 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IdType="pubmed">16348093</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>University Park (Pennsylvanie)</li></settlement><orgName><li>Université d'État de Pennsylvanie</li></orgName></list><tree><noCountry><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Pease, E A" sort="Pease, E A" uniqKey="Pease E" first="E A" last="Pease">E A Pease</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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