Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor.
Identifieur interne : 000989 ( Main/Exploration ); précédent : 000988; suivant : 000990Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor.
Auteurs : H. Ichinose [Japon] ; H. Wariishi ; H. TanakaSource :
- Applied microbiology and biotechnology [ 0175-7598 ] ; 2002.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN complémentaire (isolement et purification), ARN fongique (composition chimique), ARN fongique (génétique), Analyse de séquence d'ADN (MeSH), Basidiomycota (enzymologie), Basidiomycota (génétique), Clonage moléculaire (MeSH), Cytochromes de type c (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Masse moléculaire (MeSH), NADPH-ferrihemoprotéine reductase (biosynthèse), NADPH-ferrihemoprotéine reductase (génétique), NADPH-ferrihemoprotéine reductase (isolement et purification), Phylogenèse (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), RT-PCR (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- biosynthèse : NADPH-ferrihemoprotéine reductase.
- composition chimique : ARN fongique, Protéines recombinantes.
- enzymologie : Basidiomycota.
- génétique : ADN complémentaire, ARN fongique, Basidiomycota, Escherichia coli, NADPH-ferrihemoprotéine reductase, Protéines recombinantes.
- isolement et purification : ADN complémentaire, NADPH-ferrihemoprotéine reductase.
- métabolisme : Cytochromes de type c.
- Analyse de séquence d'ADN, Clonage moléculaire, Données de séquences moléculaires, Masse moléculaire, Phylogenèse, RT-PCR, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (enzymology), Basidiomycota (genetics), Cloning, Molecular (MeSH), Cytochrome c Group (metabolism), DNA, Complementary (genetics), DNA, Complementary (isolation & purification), Escherichia coli (genetics), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), NADPH-Ferrihemoprotein Reductase (biosynthesis), NADPH-Ferrihemoprotein Reductase (genetics), NADPH-Ferrihemoprotein Reductase (isolation & purification), Phylogeny (MeSH), RNA, Fungal (chemistry), RNA, Fungal (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , biosynthesis : NADPH-Ferrihemoprotein Reductase.
- chemical , chemistry : RNA, Fungal, Recombinant Proteins.
- chemical , genetics : DNA, Complementary, NADPH-Ferrihemoprotein Reductase, RNA, Fungal, Recombinant Proteins.
- chemical , isolation & purification : DNA, Complementary, NADPH-Ferrihemoprotein Reductase.
- chemical , metabolism : Cytochrome c Group.
- enzymology : Basidiomycota.
- genetics : Basidiomycota, Escherichia coli.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Molecular Sequence Data, Molecular Weight, Phylogeny, Reverse Transcriptase Polymerase Chain Reaction, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/ Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity.
DOI: 10.1007/s00253-002-1083-8
PubMed: 12226721
Affiliations:
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Ichinose</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Agriculture, Kyushu University, Fukuoka, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Agriculture, Kyushu University, Fukuoka</wicri:regionArea><orgName type="university">Université de Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name></author><author><name sortKey="Tanaka, H" sort="Tanaka, H" uniqKey="Tanaka H" first="H" last="Tanaka">H. Tanaka</name></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="ISSN">0175-7598</idno><imprint><date when="2002" type="published">2002</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 (enzymology)</term><term>Basidiomycota (genetics)</term><term>Cloning, Molecular (MeSH)</term><term>Cytochrome c Group (metabolism)</term><term>DNA, Complementary (genetics)</term><term>DNA, Complementary (isolation & purification)</term><term>Escherichia coli (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Weight (MeSH)</term><term>NADPH-Ferrihemoprotein Reductase (biosynthesis)</term><term>NADPH-Ferrihemoprotein Reductase (genetics)</term><term>NADPH-Ferrihemoprotein Reductase (isolation & purification)</term><term>Phylogeny (MeSH)</term><term>RNA, Fungal (chemistry)</term><term>RNA, Fungal (genetics)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>ADN complémentaire (isolement et purification)</term><term>ARN fongique (composition chimique)</term><term>ARN fongique (génétique)</term><term>Analyse de séquence d'ADN (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Basidiomycota (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Cytochromes de type c (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Masse moléculaire (MeSH)</term><term>NADPH-ferrihemoprotéine reductase (biosynthèse)</term><term>NADPH-ferrihemoprotéine reductase (génétique)</term><term>NADPH-ferrihemoprotéine reductase (isolement et purification)</term><term>Phylogenèse (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>RT-PCR (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>NADPH-Ferrihemoprotein Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA, Fungal</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>NADPH-Ferrihemoprotein Reductase</term><term>RNA, Fungal</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>DNA, Complementary</term><term>NADPH-Ferrihemoprotein Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochrome c Group</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>NADPH-ferrihemoprotéine reductase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>ARN fongique</term><term>Protéines recombinantes</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><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>ARN fongique</term><term>Basidiomycota</term><term>Escherichia coli</term><term>NADPH-ferrihemoprotéine reductase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>ADN complémentaire</term><term>NADPH-ferrihemoprotéine reductase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochromes de type c</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Phylogeny</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Sequence Analysis, DNA</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Masse moléculaire</term><term>Phylogenèse</term><term>RT-PCR</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/ Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12226721</PMID><DateCompleted><Year>2002</Year><Month>12</Month><Day>10</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0175-7598</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>6</Issue><PubDate><Year>2002</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor.</ArticleTitle><Pagination><MedlinePgn>658-64</MedlinePgn></Pagination><Abstract><AbstractText>A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/ Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ichinose</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Kyushu University, Fukuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Tanaka</LastName><ForeName>H</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>07</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003574">Cytochrome c Group</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012331">RNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.2.4</RegistryNumber><NameOfSubstance UI="D009251">NADPH-Ferrihemoprotein Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base 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="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003574" MajorTopicYN="N">Cytochrome c Group</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009251" MajorTopicYN="N">NADPH-Ferrihemoprotein Reductase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012331" MajorTopicYN="N">RNA, Fungal</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>05</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2002</Year><Month>06</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2002</Year><Month>06</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>9</Month><Day>13</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>12</Month><Day>11</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>9</Month><Day>13</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12226721</ArticleId><ArticleId IdType="doi">10.1007/s00253-002-1083-8</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><noCountry><name sortKey="Tanaka, H" sort="Tanaka, H" uniqKey="Tanaka H" first="H" last="Tanaka">H. Tanaka</name><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name></noCountry><country name="Japon"><region name="Kyūshū"><name sortKey="Ichinose, H" sort="Ichinose, H" uniqKey="Ichinose H" first="H" last="Ichinose">H. Ichinose</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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