Identification of a novel cytochrome P-450 gene from the white rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000C04 ( Main/Curation ); précédent : 000C03; suivant : 000C05Identification of a novel cytochrome P-450 gene from the white rot fungus Phanerochaete chrysosporium.
Auteurs : S W Kullman [États-Unis] ; F. MatsumuraSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1997.
Descripteurs français
- KwdFr :
- ARN fongique (analyse), Azote (métabolisme), Basidiomycota (génétique), Cadres ouverts de lecture (MeSH), Clonage moléculaire (MeSH), Cytochrome P-450 enzyme system (génétique), Données de séquences moléculaires (MeSH), Hème (génétique), Hème (immunologie), Réaction de polymérisation en chaîne (MeSH), Régulation de l'expression des gènes fongiques (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Technique de Northern (MeSH), Technique de Western (MeSH).
- MESH :
- analyse : ARN fongique.
- génétique : Basidiomycota, Cytochrome P-450 enzyme system, Hème.
- immunologie : Hème.
- métabolisme : Azote.
- Cadres ouverts de lecture, Clonage moléculaire, Données de séquences moléculaires, Réaction de polymérisation en chaîne, Régulation de l'expression des gènes fongiques, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique, Technique de Northern, Technique de Western.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (genetics), Blotting, Northern (MeSH), Blotting, Western (MeSH), Cloning, Molecular (MeSH), Cytochrome P-450 Enzyme System (genetics), Gene Expression Regulation, Fungal (MeSH), Heme (genetics), Heme (immunology), Molecular Sequence Data (MeSH), Nitrogen (metabolism), Open Reading Frames (MeSH), Polymerase Chain Reaction (MeSH), RNA, Fungal (analysis), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , analysis : RNA, Fungal.
- chemical , genetics : Cytochrome P-450 Enzyme System, Heme.
- genetics : Basidiomycota.
- chemical , immunology : Heme.
- chemical , metabolism : Nitrogen.
- Amino Acid Sequence, Base Sequence, Blotting, Northern, Blotting, Western, Cloning, Molecular, Gene Expression Regulation, Fungal, Molecular Sequence Data, Open Reading Frames, Polymerase Chain Reaction, Sequence Homology, Amino Acid.
Abstract
A gene fragment belonging to the cytochrome P-450 superfamily has been cloned and identified from stationary cultures of the filamentous fungus Phanerochaete chrysosporium by reverse transcriptase (RT)-PCR. A set of degenerate primers homologous to highly conserved regions of known cytochrome P-450 sequences were used for initial RT-PCRs. Individual PCR products were cloned, sequenced, and identified as those belonging to the cytochrome P-450 superfamily based on amino acid sequence homologies and the presence of the highly conserved heme binding region. The nucleotide sequence of a single cDNA clone indicated the presence of an open reading frame encoding a partial cytochrome P-450 protein of 208 amino acids. Comparisons of the deduced amino acid sequence of the partial protein to other known cytochrome P-450 sequences indicate that it is the first member of a new family of cytochrome P-450s, designated CYP63-1A. Northern blot analysis suggests that CYP63-1A is expressed under both nitrogen-rich and nitrogen-deficient culture conditions and thus not under the same regulatory constraints as the well-studied lignin and manganese peroxidases. Western blot analyses using antibodies raised to the heme binding region of CYP63-1A indicate that the protein has a molecular mass of approximately 44,000 Da.
DOI: 10.1128/AEM.63.7.2741-2746.1997
PubMed: 9212420
PubMed Central: PMC168569
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pubmed:9212420Le document en format XML
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<term>Blotting, Northern (MeSH)</term>
<term>Blotting, Western (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Cytochrome P-450 Enzyme System (genetics)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
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<term>Hème (génétique)</term>
<term>Hème (immunologie)</term>
<term>Réaction de polymérisation en chaîne (MeSH)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<term>Régulation de l'expression des gènes fongiques</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">A gene fragment belonging to the cytochrome P-450 superfamily has been cloned and identified from stationary cultures of the filamentous fungus Phanerochaete chrysosporium by reverse transcriptase (RT)-PCR. A set of degenerate primers homologous to highly conserved regions of known cytochrome P-450 sequences were used for initial RT-PCRs. Individual PCR products were cloned, sequenced, and identified as those belonging to the cytochrome P-450 superfamily based on amino acid sequence homologies and the presence of the highly conserved heme binding region. The nucleotide sequence of a single cDNA clone indicated the presence of an open reading frame encoding a partial cytochrome P-450 protein of 208 amino acids. Comparisons of the deduced amino acid sequence of the partial protein to other known cytochrome P-450 sequences indicate that it is the first member of a new family of cytochrome P-450s, designated CYP63-1A. Northern blot analysis suggests that CYP63-1A is expressed under both nitrogen-rich and nitrogen-deficient culture conditions and thus not under the same regulatory constraints as the well-studied lignin and manganese peroxidases. Western blot analyses using antibodies raised to the heme binding region of CYP63-1A indicate that the protein has a molecular mass of approximately 44,000 Da.</div>
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<Abstract><AbstractText>A gene fragment belonging to the cytochrome P-450 superfamily has been cloned and identified from stationary cultures of the filamentous fungus Phanerochaete chrysosporium by reverse transcriptase (RT)-PCR. A set of degenerate primers homologous to highly conserved regions of known cytochrome P-450 sequences were used for initial RT-PCRs. Individual PCR products were cloned, sequenced, and identified as those belonging to the cytochrome P-450 superfamily based on amino acid sequence homologies and the presence of the highly conserved heme binding region. The nucleotide sequence of a single cDNA clone indicated the presence of an open reading frame encoding a partial cytochrome P-450 protein of 208 amino acids. Comparisons of the deduced amino acid sequence of the partial protein to other known cytochrome P-450 sequences indicate that it is the first member of a new family of cytochrome P-450s, designated CYP63-1A. Northern blot analysis suggests that CYP63-1A is expressed under both nitrogen-rich and nitrogen-deficient culture conditions and thus not under the same regulatory constraints as the well-studied lignin and manganese peroxidases. Western blot analyses using antibodies raised to the heme binding region of CYP63-1A indicate that the protein has a molecular mass of approximately 44,000 Da.</AbstractText>
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