Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.
Identifieur interne : 000D33 ( Main/Exploration ); précédent : 000D32; suivant : 000D34Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.
Auteurs : C A Reddy [États-Unis] ; T M D'SouzaSource :
- FEMS microbiology reviews [ 0168-6445 ] ; 1994.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- génétique : Basidiomycota, Peroxidases.
- métabolisme : Lignine, Peroxidases.
- Chromosomes de champignon, Données de séquences moléculaires, Gènes fongiques, Séquence d'acides aminés, Transformation génétique.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- enzymology : Basidiomycota.
- genetics : Basidiomycota.
- Amino Acid Sequence, Chromosomes, Fungal, Genes, Fungal, Molecular Sequence Data, Transformation, Genetic.
Abstract
The white-rot basidiomycete Phanerochaete chrysosporium produces lignin peroxidases (LiPs), a family of extracellular glycosylated heme proteins, as major components of its lignin-degrading system. Up to 15 LiP isozymes, ranging in M(r) values from 38,000 to 43,000, are produced depending on culture conditions and strains employed. Manganese-dependent peroxidases (MnPs) are a second family of extracellular heme proteins produced by P. chrysosporium that are also believed to be important in lignin degradation by this organism. LiP and MnP production is seen during secondary metabolism and is completely suppressed under conditions of excess nitrogen and carbon. Excess Mn(II) in the medium, on the other hand, suppresses LiP production but enhances MnP production. Nitrogen regulation of LiP and MnP production is independent of carbon and Mn(II) regulation. LiP activity is also affected by idiophasic extracellular proteases. Intracellular cAMP levels appear to be important in regulating the production of LiPs and MnPs, although LiP production is affected more than MnP production. Studies on the sequencing and characterization of lip cDNAs and genes of P. chrysosporium have shown that the major LiP isozymes are each encoded by a separate gene. Each lip gene encodes a mature protein that is 343-344 amino acids long, contains 1 putative N-glycosylation site, a number of putative O-glycosylation sites, and is preceded by a 27-28-amino acid leader peptide ending in a Lys-Arg cleavage site. The coding region of each lip gene is interrupted by 8-9 introns (50-63 bp), and the positions of the last two introns appear to be highly conserved. There are substantial differences in the temporal transcription patterns of the major lip genes. The sequence data suggest the presence of three lip gene subfamilies. The genomic DNA of P. chrysosporium strain BKMF-1767 was resolved into 10 chromosomes (genome size of 29 Mb), and that of strain ME-446 into 11 chromosomes (genome size of 32 Mb). The lip genes have been localized to five chromosomes in BKMF-1767 and to four chromosomes in ME-446. DNA transformation studies have reported both integrative and non-integrative transformation in P. chrysosporium.
DOI: 10.1111/j.1574-6976.1994.tb00040.x
PubMed: 8167033
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.</title><author><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name><affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology, Michigan State University, East Lansing 48824-1101.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="D Souza, T M" sort="D Souza, T M" uniqKey="D Souza T" first="T M" last="D'Souza">T M D'Souza</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8167033</idno><idno type="pmid">8167033</idno><idno type="doi">10.1111/j.1574-6976.1994.tb00040.x</idno><idno type="wicri:Area/Main/Corpus">000D61</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D61</idno><idno type="wicri:Area/Main/Curation">000D61</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D61</idno><idno type="wicri:Area/Main/Exploration">000D61</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.</title><author><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name><affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology, Michigan State University, East Lansing 48824-1101.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="D Souza, T M" sort="D Souza, T M" uniqKey="D Souza T" first="T M" last="D'Souza">T M D'Souza</name></author></analytic><series><title level="j">FEMS microbiology reviews</title><idno type="ISSN">0168-6445</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Basidiomycota (genetics)</term><term>Chromosomes, Fungal (MeSH)</term><term>Genes, Fungal (MeSH)</term><term>Lignin (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Transformation, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Basidiomycota (génétique)</term><term>Chromosomes de champignon (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Lignine (métabolisme)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transformation génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" 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="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Basidiomycota</term><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>Amino Acid Sequence</term><term>Chromosomes, Fungal</term><term>Genes, Fungal</term><term>Molecular Sequence Data</term><term>Transformation, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromosomes de champignon</term><term>Données de séquences moléculaires</term><term>Gènes fongiques</term><term>Séquence d'acides aminés</term><term>Transformation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white-rot basidiomycete Phanerochaete chrysosporium produces lignin peroxidases (LiPs), a family of extracellular glycosylated heme proteins, as major components of its lignin-degrading system. Up to 15 LiP isozymes, ranging in M(r) values from 38,000 to 43,000, are produced depending on culture conditions and strains employed. Manganese-dependent peroxidases (MnPs) are a second family of extracellular heme proteins produced by P. chrysosporium that are also believed to be important in lignin degradation by this organism. LiP and MnP production is seen during secondary metabolism and is completely suppressed under conditions of excess nitrogen and carbon. Excess Mn(II) in the medium, on the other hand, suppresses LiP production but enhances MnP production. Nitrogen regulation of LiP and MnP production is independent of carbon and Mn(II) regulation. LiP activity is also affected by idiophasic extracellular proteases. Intracellular cAMP levels appear to be important in regulating the production of LiPs and MnPs, although LiP production is affected more than MnP production. Studies on the sequencing and characterization of lip cDNAs and genes of P. chrysosporium have shown that the major LiP isozymes are each encoded by a separate gene. Each lip gene encodes a mature protein that is 343-344 amino acids long, contains 1 putative N-glycosylation site, a number of putative O-glycosylation sites, and is preceded by a 27-28-amino acid leader peptide ending in a Lys-Arg cleavage site. The coding region of each lip gene is interrupted by 8-9 introns (50-63 bp), and the positions of the last two introns appear to be highly conserved. There are substantial differences in the temporal transcription patterns of the major lip genes. The sequence data suggest the presence of three lip gene subfamilies. The genomic DNA of P. chrysosporium strain BKMF-1767 was resolved into 10 chromosomes (genome size of 29 Mb), and that of strain ME-446 into 11 chromosomes (genome size of 32 Mb). The lip genes have been localized to five chromosomes in BKMF-1767 and to four chromosomes in ME-446. DNA transformation studies have reported both integrative and non-integrative transformation in P. chrysosporium.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8167033</PMID><DateCompleted><Year>1994</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0168-6445</ISSN><JournalIssue CitedMedium="Print"><Volume>13</Volume><Issue>2-3</Issue><PubDate><Year>1994</Year><Month>Mar</Month></PubDate></JournalIssue><Title>FEMS microbiology reviews</Title><ISOAbbreviation>FEMS Microbiol Rev</ISOAbbreviation></Journal><ArticleTitle>Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>137-52</MedlinePgn></Pagination><Abstract><AbstractText>The white-rot basidiomycete Phanerochaete chrysosporium produces lignin peroxidases (LiPs), a family of extracellular glycosylated heme proteins, as major components of its lignin-degrading system. Up to 15 LiP isozymes, ranging in M(r) values from 38,000 to 43,000, are produced depending on culture conditions and strains employed. Manganese-dependent peroxidases (MnPs) are a second family of extracellular heme proteins produced by P. chrysosporium that are also believed to be important in lignin degradation by this organism. LiP and MnP production is seen during secondary metabolism and is completely suppressed under conditions of excess nitrogen and carbon. Excess Mn(II) in the medium, on the other hand, suppresses LiP production but enhances MnP production. Nitrogen regulation of LiP and MnP production is independent of carbon and Mn(II) regulation. LiP activity is also affected by idiophasic extracellular proteases. Intracellular cAMP levels appear to be important in regulating the production of LiPs and MnPs, although LiP production is affected more than MnP production. Studies on the sequencing and characterization of lip cDNAs and genes of P. chrysosporium have shown that the major LiP isozymes are each encoded by a separate gene. Each lip gene encodes a mature protein that is 343-344 amino acids long, contains 1 putative N-glycosylation site, a number of putative O-glycosylation sites, and is preceded by a 27-28-amino acid leader peptide ending in a Lys-Arg cleavage site. The coding region of each lip gene is interrupted by 8-9 introns (50-63 bp), and the positions of the last two introns appear to be highly conserved. There are substantial differences in the temporal transcription patterns of the major lip genes. The sequence data suggest the presence of three lip gene subfamilies. The genomic DNA of P. chrysosporium strain BKMF-1767 was resolved into 10 chromosomes (genome size of 29 Mb), and that of strain ME-446 into 11 chromosomes (genome size of 32 Mb). The lip genes have been localized to five chromosomes in BKMF-1767 and to four chromosomes in ME-446. DNA transformation studies have reported both integrative and non-integrative transformation in P. chrysosporium.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>C A</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Michigan State University, East Lansing 48824-1101.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>D'Souza</LastName><ForeName>T M</ForeName><Initials>TM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01-GM 39032</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Microbiol Rev</MedlineTA><NlmUniqueID>8902526</NlmUniqueID><ISSNLinking>0168-6445</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>lip</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015825" MajorTopicYN="N">Chromosomes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="Y">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014170" MajorTopicYN="N">Transformation, Genetic</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>91</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>3</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8167033</ArticleId><ArticleId IdType="pii">0168-6445(94)90077-9</ArticleId><ArticleId IdType="doi">10.1111/j.1574-6976.1994.tb00040.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="D Souza, T M" sort="D Souza, T M" uniqKey="D Souza T" first="T M" last="D'Souza">T M D'Souza</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000D33 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000D33 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:8167033
|texte= Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:8167033" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |