Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000D89 ( Main/Corpus ); précédent : 000D88; suivant : 000D90Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium.
Auteurs : M H Gold ; M. AlicSource :
- Microbiological reviews [ 0146-0749 ] ; 1993.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (genetics), Basidiomycota (metabolism), Biodegradation, Environmental (MeSH), Enzyme Induction (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Genes, Fungal (MeSH), Isoenzymes (genetics), Isoenzymes (metabolism), Lignin (metabolism), Molecular Sequence Data (MeSH), Multigene Family (MeSH), Oxidation-Reduction (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Transformation, Genetic (MeSH).
- MESH :
- chemical , genetics : Fungal Proteins, Isoenzymes, Peroxidases.
- genetics : Basidiomycota.
- metabolism : Basidiomycota, Fungal Proteins, Isoenzymes, Lignin, Peroxidases.
- Amino Acid Sequence, Base Sequence, Biodegradation, Environmental, Enzyme Induction, Gene Expression Regulation, Fungal, Genes, Fungal, Molecular Sequence Data, Multigene Family, Oxidation-Reduction, Sequence Alignment, Sequence Homology, Amino Acid, Transformation, Genetic.
Abstract
The white rot basidiomycete Phanerochaete chrysosporium completely degrades lignin and a variety of aromatic pollutants during the secondary metabolic phase of growth. Two families of secreted heme enzymes, lignin peroxidase (LiP) and manganese peroxidase (MnP), are major components of the extracellular lignin degradative system of this organism. MnP and LiP both are encoded by families of genes, and the lip genes appear to be clustered. The lip genes contain eight or nine short introns; the mnp genes contain six or seven short introns. The sequences surrounding active-site residues are conserved among LiP, MnP, cytochrome c peroxidase, and plant peroxidases. The eight LiP cysteine residues align with 8 of the 10 cysteines in MnP. LiPs are synthesized as preproenzymes with a 21-amino-acid signal sequence followed by a 6- or 7-amino-acid propeptide. MnPs have a 21- or 24-amino-acid signal sequence but apparently lack a propeptide. Both LiP and MnP are regulated at the mRNA level by nitrogen, and the various isozymes may be differentially regulated by carbon and nitrogen. MnP also is regulated at the level of gene transcription by Mn(II), the substrate for the enzyme, and by heat shock. The promoter regions of mnp genes contain multiple heat shock elements as well as sequences that are identical to the consensus metal regulatory elements found in mammalian metallothionein genes. DNA transformation systems have been developed for P. chrysosporium and are being used for studies on gene regulation and for gene replacement experiments.
PubMed: 8246842
PubMed Central: PMC372928
Links to Exploration step
pubmed:8246842Le document en format XML
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Alic</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8246842</idno><idno type="pmid">8246842</idno><idno type="pmc">PMC372928</idno><idno type="wicri:Area/Main/Corpus">000D89</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D89</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium.</title><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><affiliation><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000.</nlm:affiliation></affiliation></author><author><name sortKey="Alic, M" sort="Alic, M" uniqKey="Alic M" first="M" last="Alic">M. Alic</name></author></analytic><series><title level="j">Microbiological reviews</title><idno type="ISSN">0146-0749</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Basidiomycota (genetics)</term><term>Basidiomycota (metabolism)</term><term>Biodegradation, Environmental (MeSH)</term><term>Enzyme Induction (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Genes, Fungal (MeSH)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Lignin (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Multigene Family (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Transformation, Genetic (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term><term>Fungal Proteins</term><term>Isoenzymes</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Biodegradation, Environmental</term><term>Enzyme Induction</term><term>Gene Expression Regulation, Fungal</term><term>Genes, Fungal</term><term>Molecular Sequence Data</term><term>Multigene Family</term><term>Oxidation-Reduction</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Transformation, Genetic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white rot basidiomycete Phanerochaete chrysosporium completely degrades lignin and a variety of aromatic pollutants during the secondary metabolic phase of growth. Two families of secreted heme enzymes, lignin peroxidase (LiP) and manganese peroxidase (MnP), are major components of the extracellular lignin degradative system of this organism. MnP and LiP both are encoded by families of genes, and the lip genes appear to be clustered. The lip genes contain eight or nine short introns; the mnp genes contain six or seven short introns. The sequences surrounding active-site residues are conserved among LiP, MnP, cytochrome c peroxidase, and plant peroxidases. The eight LiP cysteine residues align with 8 of the 10 cysteines in MnP. LiPs are synthesized as preproenzymes with a 21-amino-acid signal sequence followed by a 6- or 7-amino-acid propeptide. MnPs have a 21- or 24-amino-acid signal sequence but apparently lack a propeptide. Both LiP and MnP are regulated at the mRNA level by nitrogen, and the various isozymes may be differentially regulated by carbon and nitrogen. MnP also is regulated at the level of gene transcription by Mn(II), the substrate for the enzyme, and by heat shock. The promoter regions of mnp genes contain multiple heat shock elements as well as sequences that are identical to the consensus metal regulatory elements found in mammalian metallothionein genes. DNA transformation systems have been developed for P. chrysosporium and are being used for studies on gene regulation and for gene replacement experiments.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8246842</PMID><DateCompleted><Year>1994</Year><Month>01</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0146-0749</ISSN><JournalIssue CitedMedium="Print"><Volume>57</Volume><Issue>3</Issue><PubDate><Year>1993</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Microbiological reviews</Title><ISOAbbreviation>Microbiol Rev</ISOAbbreviation></Journal><ArticleTitle>Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>605-22</MedlinePgn></Pagination><Abstract><AbstractText>The white rot basidiomycete Phanerochaete chrysosporium completely degrades lignin and a variety of aromatic pollutants during the secondary metabolic phase of growth. Two families of secreted heme enzymes, lignin peroxidase (LiP) and manganese peroxidase (MnP), are major components of the extracellular lignin degradative system of this organism. MnP and LiP both are encoded by families of genes, and the lip genes appear to be clustered. The lip genes contain eight or nine short introns; the mnp genes contain six or seven short introns. The sequences surrounding active-site residues are conserved among LiP, MnP, cytochrome c peroxidase, and plant peroxidases. The eight LiP cysteine residues align with 8 of the 10 cysteines in MnP. LiPs are synthesized as preproenzymes with a 21-amino-acid signal sequence followed by a 6- or 7-amino-acid propeptide. MnPs have a 21- or 24-amino-acid signal sequence but apparently lack a propeptide. Both LiP and MnP are regulated at the mRNA level by nitrogen, and the various isozymes may be differentially regulated by carbon and nitrogen. MnP also is regulated at the level of gene transcription by Mn(II), the substrate for the enzyme, and by heat shock. The promoter regions of mnp genes contain multiple heat shock elements as well as sequences that are identical to the consensus metal regulatory elements found in mammalian metallothionein genes. DNA transformation systems have been developed for P. chrysosporium and are being used for studies on gene regulation and for gene replacement experiments.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alic</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><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 UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005810" MajorTopicYN="N">Multigene Family</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014170" MajorTopicYN="N">Transformation, 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