Serveur d'exploration sur le phanerochaete

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A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia radiata: characterization and expression in Trichoderma reesei.

Identifieur interne : 000F98 ( Main/Exploration ); précédent : 000F97; suivant : 000F99

A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia radiata: characterization and expression in Trichoderma reesei.

Auteurs : M. Saloheimo [Finlande] ; V. Barajas ; M L Niku-Paavola ; J K Knowles

Source :

RBID : pubmed:2628172

Descripteurs français

English descriptors

Abstract

The nucleotide sequence of a cDNA coding for a lignin peroxidase (Lgp) of the white-rot fungus, Phlebia radiata, has been determined. By amino acid (aa) sequencing, it has been shown that the protein product of this gene is the LIII Lgp of Pb. radiata. The isolated gene and the putative aa sequence are about 60% homologous to published Lgp sequences from the fungus, Phanerochaete chrysosporium. The aa thought to be involved in the catalysis of LIII are revealed by comparison with the yeast cytochrome c peroxidase. The P. radiata Lgp-encoding gene (lgp3) was expressed in the fungus, Trichoderma reesei, under the cellobiohydrolase-encoding cbh1 gene promoter. Lgp3 mRNA was produced by the T. reesei transformants. No Lgp protein, however, could be detected.

DOI: 10.1016/0378-1119(89)90427-7
PubMed: 2628172


Affiliations:


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Le document en format XML

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<title xml:lang="en">A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia radiata: characterization and expression in Trichoderma reesei.</title>
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<name sortKey="Saloheimo, M" sort="Saloheimo, M" uniqKey="Saloheimo M" first="M" last="Saloheimo">M. Saloheimo</name>
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<nlm:affiliation>VTT, Biotechnical Laboratory, Espoo, Finland.</nlm:affiliation>
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<wicri:regionArea>VTT, Biotechnical Laboratory, Espoo</wicri:regionArea>
<wicri:noRegion>Espoo</wicri:noRegion>
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<name sortKey="Barajas, V" sort="Barajas, V" uniqKey="Barajas V" first="V" last="Barajas">V. Barajas</name>
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<name sortKey="Niku Paavola, M L" sort="Niku Paavola, M L" uniqKey="Niku Paavola M" first="M L" last="Niku-Paavola">M L Niku-Paavola</name>
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<name sortKey="Knowles, J K" sort="Knowles, J K" uniqKey="Knowles J" first="J K" last="Knowles">J K Knowles</name>
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<term>Agaricales (enzymology)</term>
<term>Agaricales (genetics)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Blotting, Northern (MeSH)</term>
<term>DNA, Fungal (genetics)</term>
<term>Gene Library (MeSH)</term>
<term>Genes, Fungal (MeSH)</term>
<term>Mitosporic Fungi (genetics)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Peroxidases (genetics)</term>
<term>Plasmids (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Sequence Homology, Nucleic Acid (MeSH)</term>
<term>Trichoderma (enzymology)</term>
<term>Trichoderma (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>ADN fongique (génétique)</term>
<term>Agaricales (enzymologie)</term>
<term>Agaricales (génétique)</term>
<term>Banque de gènes (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Deuteromycota (génétique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Gènes fongiques (MeSH)</term>
<term>Peroxidases (génétique)</term>
<term>Plasmides (MeSH)</term>
<term>Similitude de séquences d'acides nucléiques (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Technique de Northern (MeSH)</term>
<term>Trichoderma (enzymologie)</term>
<term>Trichoderma (génétique)</term>
</keywords>
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<term>DNA, Fungal</term>
<term>Peroxidases</term>
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<term>Agaricales</term>
<term>Trichoderma</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Agaricales</term>
<term>Trichoderma</term>
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<term>Agaricales</term>
<term>Mitosporic Fungi</term>
<term>Trichoderma</term>
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<term>ADN fongique</term>
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<term>Deuteromycota</term>
<term>Peroxidases</term>
<term>Trichoderma</term>
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<term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Blotting, Northern</term>
<term>Gene Library</term>
<term>Genes, Fungal</term>
<term>Molecular Sequence Data</term>
<term>Plasmids</term>
<term>Protein Conformation</term>
<term>Sequence Homology, Nucleic Acid</term>
</keywords>
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<term>Banque de gènes</term>
<term>Conformation des protéines</term>
<term>Données de séquences moléculaires</term>
<term>Gènes fongiques</term>
<term>Plasmides</term>
<term>Similitude de séquences d'acides nucléiques</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Technique de Northern</term>
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<front>
<div type="abstract" xml:lang="en">The nucleotide sequence of a cDNA coding for a lignin peroxidase (Lgp) of the white-rot fungus, Phlebia radiata, has been determined. By amino acid (aa) sequencing, it has been shown that the protein product of this gene is the LIII Lgp of Pb. radiata. The isolated gene and the putative aa sequence are about 60% homologous to published Lgp sequences from the fungus, Phanerochaete chrysosporium. The aa thought to be involved in the catalysis of LIII are revealed by comparison with the yeast cytochrome c peroxidase. The P. radiata Lgp-encoding gene (lgp3) was expressed in the fungus, Trichoderma reesei, under the cellobiohydrolase-encoding cbh1 gene promoter. Lgp3 mRNA was produced by the T. reesei transformants. No Lgp protein, however, could be detected.</div>
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<Issue>2</Issue>
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<AbstractText>The nucleotide sequence of a cDNA coding for a lignin peroxidase (Lgp) of the white-rot fungus, Phlebia radiata, has been determined. By amino acid (aa) sequencing, it has been shown that the protein product of this gene is the LIII Lgp of Pb. radiata. The isolated gene and the putative aa sequence are about 60% homologous to published Lgp sequences from the fungus, Phanerochaete chrysosporium. The aa thought to be involved in the catalysis of LIII are revealed by comparison with the yeast cytochrome c peroxidase. The P. radiata Lgp-encoding gene (lgp3) was expressed in the fungus, Trichoderma reesei, under the cellobiohydrolase-encoding cbh1 gene promoter. Lgp3 mRNA was produced by the T. reesei transformants. No Lgp protein, however, could be detected.</AbstractText>
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