PoplarV1, Main, Curation, bibRecord, 004936

Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar.

Identifieur interne : 004936 ( Main/Curation ); précédent : 004935; suivant : 004937

Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar.

Auteurs : P. Ranocha [France] ; G. Mcdougall ; S. Hawkins ; R. Sterjiades ; G. Borderies ; D. Stewart ; M. Cabanes-Macheteau ; A M Boudet ; D. Goffner

Source :

European journal of biochemistry [ 0014-2956 ] ; 1999.

RBID : pubmed:9914531

Descripteurs français

English descriptors

KwdEn :
- Acrolein (analogs & derivatives), Acrolein (metabolism), Amino Acid Sequence (MeSH), Cell Wall (enzymology), Cloning, Molecular (MeSH), Copper (MeSH), Evolution, Molecular (MeSH), Genes, Plant (MeSH), Glycoproteins (genetics), Glycoproteins (metabolism), Laccase (MeSH), Lignin (metabolism), Magnoliopsida (enzymology), Magnoliopsida (genetics), Metalloproteins (genetics), Metalloproteins (metabolism), Molecular Sequence Data (MeSH), Monophenol Monooxygenase (genetics), Monophenol Monooxygenase (metabolism), Multigene Family (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Phenols (metabolism), Plant Stems (enzymology), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Trees (enzymology), Trees (genetics).
MESH :
- chemical , analogs & derivatives : Acrolein.
- chemical , genetics : Glycoproteins, Metalloproteins, Monophenol Monooxygenase, Oxidoreductases.
- chemical , metabolism : Acrolein, Glycoproteins, Lignin, Metalloproteins, Monophenol Monooxygenase, Oxidoreductases, Phenols.
- enzymology : Cell Wall, Magnoliopsida, Plant Stems, Trees.
- genetics : Magnoliopsida, Trees.
- Amino Acid Sequence, Cloning, Molecular, Copper, Evolution, Molecular, Genes, Plant, Laccase, Molecular Sequence Data, Multigene Family, Sequence Homology, Amino Acid, Substrate Specificity.

Abstract

The nature of the enzyme(s) involved in the dehydrogenative polymerization of lignin monomers is still a matter of debate. Potential candidates include laccases which have recently received attention due to their capacity to oxidize lignin monomers and close spatial and temporal correlation with lignin deposition. We have characterized two H2O2-independent phenoloxidases with approximate molecular masses of 90 kDa and 110 kDa from cell walls of Populus euramericana xylem that are capable of oxidizing coniferyl alcohol. The 90-kDa protein was purified to apparent homogeneity and extensively characterized at the biochemical and structural levels. To our knowledge, this is the first report of a plant laccase purified to homogeneity from a lignifying tissue of an angiosperm. The cDNA clones corresponding to the 90-kDa and 110-kDa proteins, lac90 and lac110, were obtained by a PCR-based approach using specific oligonucleotides derived from peptide sequences. Sequence analysis indicated that lac90 and lac110 encoded two distinct laccases. In addition, heterologous screening using an Acer pseudoplatanus laccase cDNA enabled us to obtain three additional cDNAs (lac1, lac2, lac3) that did not correspond to lac90 and lac110. The five laccase cDNAs correspond to a highly divergent multigene family but Northern analysis with gene-specific probes indicated that all of the genes are exclusively and abundantly expressed in stems. These results highlight the polymorphism of plant laccases by an integrated biochemical and molecular approach, and provide the tools that will enable us to clearly determine the function of these enzymes in plants by molecular and genetic approaches.

DOI: 10.1046/j.1432-1327.1999.00061.x
PubMed: 9914531

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Le document en format XML

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<author><name sortKey="Cabanes Macheteau, M" sort="Cabanes Macheteau, M" uniqKey="Cabanes Macheteau M" first="M" last="Cabanes-Macheteau">M. Cabanes-Macheteau</name>
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<term>Acrolein (metabolism)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Cell Wall (enzymology)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Copper (MeSH)</term>
<term>Evolution, Molecular (MeSH)</term>
<term>Genes, Plant (MeSH)</term>
<term>Glycoproteins (genetics)</term>
<term>Glycoproteins (metabolism)</term>
<term>Laccase (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Magnoliopsida (enzymology)</term>
<term>Magnoliopsida (genetics)</term>
<term>Metalloproteins (genetics)</term>
<term>Metalloproteins (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Monophenol Monooxygenase (genetics)</term>
<term>Monophenol Monooxygenase (metabolism)</term>
<term>Multigene Family (MeSH)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phenols (metabolism)</term>
<term>Plant Stems (enzymology)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Trees (enzymology)</term>
<term>Trees (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acroléine (analogues et dérivés)</term>
<term>Acroléine (métabolisme)</term>
<term>Arbres (enzymologie)</term>
<term>Arbres (génétique)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Cuivre (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Famille multigénique (MeSH)</term>
<term>Glycoprotéines (génétique)</term>
<term>Glycoprotéines (métabolisme)</term>
<term>Gènes de plante (MeSH)</term>
<term>Laccase (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Magnoliopsida (enzymologie)</term>
<term>Magnoliopsida (génétique)</term>
<term>Monophenol monooxygenase (génétique)</term>
<term>Monophenol monooxygenase (métabolisme)</term>
<term>Métalloprotéines (génétique)</term>
<term>Métalloprotéines (métabolisme)</term>
<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Paroi cellulaire (enzymologie)</term>
<term>Phénols (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Tiges de plante (enzymologie)</term>
<term>Évolution moléculaire (MeSH)</term>
</keywords>
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</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycoproteins</term>
<term>Metalloproteins</term>
<term>Monophenol Monooxygenase</term>
<term>Oxidoreductases</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acrolein</term>
<term>Glycoproteins</term>
<term>Lignin</term>
<term>Metalloproteins</term>
<term>Monophenol Monooxygenase</term>
<term>Oxidoreductases</term>
<term>Phenols</term>
</keywords>
<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acroléine</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arbres</term>
<term>Magnoliopsida</term>
<term>Paroi cellulaire</term>
<term>Tiges de plante</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Wall</term>
<term>Magnoliopsida</term>
<term>Plant Stems</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Magnoliopsida</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arbres</term>
<term>Glycoprotéines</term>
<term>Magnoliopsida</term>
<term>Monophenol monooxygenase</term>
<term>Métalloprotéines</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acroléine</term>
<term>Glycoprotéines</term>
<term>Lignine</term>
<term>Monophenol monooxygenase</term>
<term>Métalloprotéines</term>
<term>Oxidoreductases</term>
<term>Phénols</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Cloning, Molecular</term>
<term>Copper</term>
<term>Evolution, Molecular</term>
<term>Genes, Plant</term>
<term>Laccase</term>
<term>Molecular Sequence Data</term>
<term>Multigene Family</term>
<term>Sequence Homology, Amino Acid</term>
<term>Substrate Specificity</term>
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<term>Cuivre</term>
<term>Données de séquences moléculaires</term>
<term>Famille multigénique</term>
<term>Gènes de plante</term>
<term>Laccase</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Spécificité du substrat</term>
<term>Séquence d'acides aminés</term>
<term>Évolution moléculaire</term>
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<front><div type="abstract" xml:lang="en">The nature of the enzyme(s) involved in the dehydrogenative polymerization of lignin monomers is still a matter of debate. Potential candidates include laccases which have recently received attention due to their capacity to oxidize lignin monomers and close spatial and temporal correlation with lignin deposition. We have characterized two H2O2-independent phenoloxidases with approximate molecular masses of 90 kDa and 110 kDa from cell walls of Populus euramericana xylem that are capable of oxidizing coniferyl alcohol. The 90-kDa protein was purified to apparent homogeneity and extensively characterized at the biochemical and structural levels. To our knowledge, this is the first report of a plant laccase purified to homogeneity from a lignifying tissue of an angiosperm. The cDNA clones corresponding to the 90-kDa and 110-kDa proteins, lac90 and lac110, were obtained by a PCR-based approach using specific oligonucleotides derived from peptide sequences. Sequence analysis indicated that lac90 and lac110 encoded two distinct laccases. In addition, heterologous screening using an Acer pseudoplatanus laccase cDNA enabled us to obtain three additional cDNAs (lac1, lac2, lac3) that did not correspond to lac90 and lac110. The five laccase cDNAs correspond to a highly divergent multigene family but Northern analysis with gene-specific probes indicated that all of the genes are exclusively and abundantly expressed in stems. These results highlight the polymorphism of plant laccases by an integrated biochemical and molecular approach, and provide the tools that will enable us to clearly determine the function of these enzymes in plants by molecular and genetic approaches.</div>
</front>
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<Abstract><AbstractText>The nature of the enzyme(s) involved in the dehydrogenative polymerization of lignin monomers is still a matter of debate. Potential candidates include laccases which have recently received attention due to their capacity to oxidize lignin monomers and close spatial and temporal correlation with lignin deposition. We have characterized two H2O2-independent phenoloxidases with approximate molecular masses of 90 kDa and 110 kDa from cell walls of Populus euramericana xylem that are capable of oxidizing coniferyl alcohol. The 90-kDa protein was purified to apparent homogeneity and extensively characterized at the biochemical and structural levels. To our knowledge, this is the first report of a plant laccase purified to homogeneity from a lignifying tissue of an angiosperm. The cDNA clones corresponding to the 90-kDa and 110-kDa proteins, lac90 and lac110, were obtained by a PCR-based approach using specific oligonucleotides derived from peptide sequences. Sequence analysis indicated that lac90 and lac110 encoded two distinct laccases. In addition, heterologous screening using an Acer pseudoplatanus laccase cDNA enabled us to obtain three additional cDNAs (lac1, lac2, lac3) that did not correspond to lac90 and lac110. The five laccase cDNAs correspond to a highly divergent multigene family but Northern analysis with gene-specific probes indicated that all of the genes are exclusively and abundantly expressed in stems. These results highlight the polymorphism of plant laccases by an integrated biochemical and molecular approach, and provide the tools that will enable us to clearly determine the function of these enzymes in plants by molecular and genetic approaches.</AbstractText>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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   |texte=   Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar.
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Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar.

Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar.

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