PoplarV1, Main, Exploration, bibRecord, 004614

Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar.

Identifieur interne : 004614 ( Main/Exploration ); précédent : 004613; suivant : 004615

Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar.

Auteurs : Dae-Kyun Ro [Canada] ; Jürgen Ehlting ; Carl J. Douglas

Source :

Plant physiology [ 0032-0889 ] ; 2002.

RBID : pubmed:12481067

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (genetics), Arabidopsis (metabolism), Cloning, Molecular (MeSH), Endoplasmic Reticulum (genetics), Endoplasmic Reticulum (metabolism), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Green Fluorescent Proteins (MeSH), Hybrid Vigor (genetics), Isoenzymes (genetics), Isoenzymes (metabolism), Luminescent Proteins (genetics), Luminescent Proteins (metabolism), Molecular Sequence Data (MeSH), NADPH-Ferrihemoprotein Reductase (genetics), NADPH-Ferrihemoprotein Reductase (metabolism), Phylogeny (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Plants, Genetically Modified (MeSH), Populus (enzymology), Populus (genetics), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , genetics : Isoenzymes, Luminescent Proteins, NADPH-Ferrihemoprotein Reductase, Plant Proteins, Recombinant Fusion Proteins.
- chemical , metabolism : Isoenzymes, Luminescent Proteins, NADPH-Ferrihemoprotein Reductase, Plant Proteins, Recombinant Fusion Proteins.
- chemical : Green Fluorescent Proteins.
- enzymology : Populus.
- genetics : Arabidopsis, Endoplasmic Reticulum, Hybrid Vigor, Populus, Saccharomyces cerevisiae.
- metabolism : Arabidopsis, Endoplasmic Reticulum, Saccharomyces cerevisiae.
- Amino Acid Sequence, Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Molecular Sequence Data, Phylogeny, Plants, Genetically Modified, Sequence Homology, Amino Acid.

Abstract

NADPH:cytochrome P450 reductase (CPR) provides reducing equivalents to diverse cytochrome P450 monooxygenases. We isolated cDNAs for three CPR genes (CPR1, CPR2, and CPR3) from hybrid poplar (Populus trichocarpa x Populus deltoides). Deduced CPR2 and CPR3 amino acid sequences were 91% identical, but encoded isoforms divergent from CPR1 (72% identity). CPR1 and CPR2 were co-expressed together with the P450 enzyme cinnamate-4-hydroxylase (C4H) in yeast (Saccharomyces cerevisiae). Microsomes isolated from strains expressing CPR1/C4H or CPR2/C4H enhanced C4H activities approximately 10-fold relative to the C4H-only control strain, and catalyzed NADPH-dependent cytochrome c reduction. The divergent CPR isoforms (CPR1 and CPR2/3) contained entirely different N-terminal sequences, which are conserved in other plant CPRs and are diagnostic for two distinct classes of CPRs within the angiosperms. C-terminal green fluorescent protein fusions to CPR1 and CPR2 were constructed and expressed in both yeast and Arabidopsis. The fusion proteins expressed in yeast retained the ability to support C4H activity and, thus, were catalytically active. Both CPR::green fluorescent protein fusion proteins were strictly localized to the endoplasmic reticulum in transgenic Arabidopsis. The lack of localization of either isoform to chloroplasts, where P450s are known to be present, suggests that an alternative P450 reduction system may be operative in this organelle. Transcripts for the three poplar CPR genes were present ubiquitously in all tissues examined, but CPR2 showed highest expression in young leaf tissue.

DOI: 10.1104/pp.008011
PubMed: 12481067
PubMed Central: PMC166695

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Protéines de fusion recombinantes (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">NADPH:cytochrome P450 reductase (CPR) provides reducing equivalents to diverse cytochrome P450 monooxygenases. We isolated cDNAs for three CPR genes (CPR1, CPR2, and CPR3) from hybrid poplar (Populus trichocarpa x Populus deltoides). Deduced CPR2 and CPR3 amino acid sequences were 91% identical, but encoded isoforms divergent from CPR1 (72% identity). CPR1 and CPR2 were co-expressed together with the P450 enzyme cinnamate-4-hydroxylase (C4H) in yeast (Saccharomyces cerevisiae). Microsomes isolated from strains expressing CPR1/C4H or CPR2/C4H enhanced C4H activities approximately 10-fold relative to the C4H-only control strain, and catalyzed NADPH-dependent cytochrome c reduction. The divergent CPR isoforms (CPR1 and CPR2/3) contained entirely different N-terminal sequences, which are conserved in other plant CPRs and are diagnostic for two distinct classes of CPRs within the angiosperms. C-terminal green fluorescent protein fusions to CPR1 and CPR2 were constructed and expressed in both yeast and Arabidopsis. The fusion proteins expressed in yeast retained the ability to support C4H activity and, thus, were catalytically active. Both CPR::green fluorescent protein fusion proteins were strictly localized to the endoplasmic reticulum in transgenic Arabidopsis. The lack of localization of either isoform to chloroplasts, where P450s are known to be present, suggests that an alternative P450 reduction system may be operative in this organelle. Transcripts for the three poplar CPR genes were present ubiquitously in all tissues examined, but CPR2 showed highest expression in young leaf tissue.</div>
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<Abstract><AbstractText>NADPH:cytochrome P450 reductase (CPR) provides reducing equivalents to diverse cytochrome P450 monooxygenases. We isolated cDNAs for three CPR genes (CPR1, CPR2, and CPR3) from hybrid poplar (Populus trichocarpa x Populus deltoides). Deduced CPR2 and CPR3 amino acid sequences were 91% identical, but encoded isoforms divergent from CPR1 (72% identity). CPR1 and CPR2 were co-expressed together with the P450 enzyme cinnamate-4-hydroxylase (C4H) in yeast (Saccharomyces cerevisiae). Microsomes isolated from strains expressing CPR1/C4H or CPR2/C4H enhanced C4H activities approximately 10-fold relative to the C4H-only control strain, and catalyzed NADPH-dependent cytochrome c reduction. The divergent CPR isoforms (CPR1 and CPR2/3) contained entirely different N-terminal sequences, which are conserved in other plant CPRs and are diagnostic for two distinct classes of CPRs within the angiosperms. C-terminal green fluorescent protein fusions to CPR1 and CPR2 were constructed and expressed in both yeast and Arabidopsis. The fusion proteins expressed in yeast retained the ability to support C4H activity and, thus, were catalytically active. Both CPR::green fluorescent protein fusion proteins were strictly localized to the endoplasmic reticulum in transgenic Arabidopsis. The lack of localization of either isoform to chloroplasts, where P450s are known to be present, suggests that an alternative P450 reduction system may be operative in this organelle. Transcripts for the three poplar CPR genes were present ubiquitously in all tissues examined, but CPR2 showed highest expression in young leaf tissue.</AbstractText>
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Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar.

Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar.

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