PoplarV1, Main, Exploration, bibRecord, 004702

Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase.

Identifieur interne : 004702 ( Main/Exploration ); précédent : 004701; suivant : 004703

Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase.

Auteurs : D K Ro [Canada] ; N. Mah ; B E Ellis ; C J Douglas

Source :

Plant physiology [ 0032-0889 ] ; 2001.

RBID : pubmed:11351095

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Artificial Gene Fusion (MeSH), Base Sequence (MeSH), Catalysis (MeSH), Cytochrome P-450 Enzyme System (chemistry), Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), DNA Primers (MeSH), DNA, Complementary (MeSH), Green Fluorescent Proteins (MeSH), Luminescent Proteins (genetics), Mixed Function Oxygenases (chemistry), Mixed Function Oxygenases (genetics), Mixed Function Oxygenases (metabolism), Molecular Sequence Data (MeSH), RNA, Plant (metabolism), Sequence Homology, Amino Acid (MeSH), Subcellular Fractions (enzymology), Trans-Cinnamate 4-Monooxygenase (MeSH), Trees (enzymology).
MESH :
- chemical , chemistry : Cytochrome P-450 Enzyme System, Mixed Function Oxygenases.
- chemical , genetics : Cytochrome P-450 Enzyme System, Luminescent Proteins, Mixed Function Oxygenases.
- chemical , metabolism : Cytochrome P-450 Enzyme System, Mixed Function Oxygenases, RNA, Plant.
- enzymology : Subcellular Fractions, Trees.
- Amino Acid Sequence, Artificial Gene Fusion, Base Sequence, Catalysis, DNA Primers, DNA, Complementary, Green Fluorescent Proteins, Molecular Sequence Data, Sequence Homology, Amino Acid, Trans-Cinnamate 4-Monooxygenase.

Abstract

Cinnamic acid 4-hydroxylase (C4H), a member of the cytochrome P450 monooxygenase superfamily, plays a central role in phenylpropanoid metabolism and lignin biosynthesis and possibly anchors a phenylpropanoid enzyme complex to the endoplasmic reticulum (ER). A full-length cDNA encoding C4H was isolated from a hybrid poplar (Populus trichocarpa x P. deltoides) young leaf cDNA library. RNA-blot analysis detected C4H transcripts in all organs tested, but the gene was most highly expressed in developing xylem. C4H expression was also strongly induced by elicitor-treatment in poplar cell cultures. To verify the catalytic activity of the putative C4H cDNA, two constructs, C4H and C4H fused to the FLAG epitope (C4H::FLAG), were expressed in yeast. Immunoblot analysis showed that C4H was present in the microsomal fraction and microsomal preparations from strains expressing both enzymes efficiently converted cinnamic acid to p-coumaric acid with high specific activities. To investigate the subcellular localization of C4H in vivo, a chimeric C4H-green fluorescent protein (GFP) gene was engineered and stably expressed in Arabidopsis. Confocal laser microscopy analysis clearly showed that in Arabidopsis the C4H::GFP chimeric enzyme was localized to the ER. When expressed in yeast, the C4H::GFP fusion enzyme was also active but displayed significantly lower specific activity than either C4H or C4H::FLAG in in vitro and in vivo enzyme assays. These data definitively show that C4H is localized to the ER in planta.

DOI: 10.1104/pp.126.1.317
PubMed: 11351095
PubMed Central: PMC102306

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Cinnamic acid 4-hydroxylase (C4H), a member of the cytochrome P450 monooxygenase superfamily, plays a central role in phenylpropanoid metabolism and lignin biosynthesis and possibly anchors a phenylpropanoid enzyme complex to the endoplasmic reticulum (ER). A full-length cDNA encoding C4H was isolated from a hybrid poplar (Populus trichocarpa x P. deltoides) young leaf cDNA library. RNA-blot analysis detected C4H transcripts in all organs tested, but the gene was most highly expressed in developing xylem. C4H expression was also strongly induced by elicitor-treatment in poplar cell cultures. To verify the catalytic activity of the putative C4H cDNA, two constructs, C4H and C4H fused to the FLAG epitope (C4H::FLAG), were expressed in yeast. Immunoblot analysis showed that C4H was present in the microsomal fraction and microsomal preparations from strains expressing both enzymes efficiently converted cinnamic acid to p-coumaric acid with high specific activities. To investigate the subcellular localization of C4H in vivo, a chimeric C4H-green fluorescent protein (GFP) gene was engineered and stably expressed in Arabidopsis. Confocal laser microscopy analysis clearly showed that in Arabidopsis the C4H::GFP chimeric enzyme was localized to the ER. When expressed in yeast, the C4H::GFP fusion enzyme was also active but displayed significantly lower specific activity than either C4H or C4H::FLAG in in vitro and in vivo enzyme assays. These data definitively show that C4H is localized to the ER in planta.</div>
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<Abstract><AbstractText>Cinnamic acid 4-hydroxylase (C4H), a member of the cytochrome P450 monooxygenase superfamily, plays a central role in phenylpropanoid metabolism and lignin biosynthesis and possibly anchors a phenylpropanoid enzyme complex to the endoplasmic reticulum (ER). A full-length cDNA encoding C4H was isolated from a hybrid poplar (Populus trichocarpa x P. deltoides) young leaf cDNA library. RNA-blot analysis detected C4H transcripts in all organs tested, but the gene was most highly expressed in developing xylem. C4H expression was also strongly induced by elicitor-treatment in poplar cell cultures. To verify the catalytic activity of the putative C4H cDNA, two constructs, C4H and C4H fused to the FLAG epitope (C4H::FLAG), were expressed in yeast. Immunoblot analysis showed that C4H was present in the microsomal fraction and microsomal preparations from strains expressing both enzymes efficiently converted cinnamic acid to p-coumaric acid with high specific activities. To investigate the subcellular localization of C4H in vivo, a chimeric C4H-green fluorescent protein (GFP) gene was engineered and stably expressed in Arabidopsis. Confocal laser microscopy analysis clearly showed that in Arabidopsis the C4H::GFP chimeric enzyme was localized to the ER. When expressed in yeast, the C4H::GFP fusion enzyme was also active but displayed significantly lower specific activity than either C4H or C4H::FLAG in in vitro and in vivo enzyme assays. These data definitively show that C4H is localized to the ER in planta.</AbstractText>
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Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase.

Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase.

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