Serveur d'exploration sur le phanerochaete

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Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase gene.

Identifieur interne : 001009 ( Main/Exploration ); précédent : 001008; suivant : 001010

Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase gene.

Auteurs : I. Walther [Suisse] ; M. K Lin ; J. Reiser ; F. Suter ; B. Fritsche ; M. Saloheimo ; M. Leisola ; T. Teeri ; J K Knowles ; A. Fiechter

Source :

RBID : pubmed:3240864

Descripteurs français

English descriptors

Abstract

The basidiomycete fungus Phanerochaete chrysosporium produces a number of extracellular peroxidases which appear to be important for lignin degradation. We present here the isolation and complete nucleotide (nt) sequence of a gene (lpo) coding for lignin peroxidase (LPO), the coding region of which is identical to a lpo cDNA sequence which had previously been described [M. Tien and C.-P.D. Tu, Nature 326 (1987) 520-523]. The deduced amino acid (aa) sequence corresponds to 372 aa residues and the coding region is interrupted by eight short introns that range in size from 50 to 62 nt. Southern blot experiments using the cloned lpo gene as hybridization probe revealed a complex restriction fragment pattern, indicating that there are a number of lpo-related nucleotide sequences present in P. chrysosporium DNA which cross-hybridize. We also present data on the in vivo expression of the lpo genes and show that they are regulated at the RNA level and that the structure of the transcripts as judged from S1 experiments is complex. These data are consistent with the idea that there are a number of related lpo genes in P. chrysosporium which constitute a gene family.

DOI: 10.1016/0378-1119(88)90111-4
PubMed: 3240864


Affiliations:


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Le document en format XML

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<term>Base Sequence (MeSH)</term>
<term>Chrysosporium (enzymology)</term>
<term>Chrysosporium (genetics)</term>
<term>Clone Cells (analysis)</term>
<term>DNA (analysis)</term>
<term>DNA, Fungal (genetics)</term>
<term>Genes (MeSH)</term>
<term>Mitosporic Fungi (genetics)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxygenases (genetics)</term>
<term>Restriction Mapping (MeSH)</term>
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<term>ADN (analyse)</term>
<term>ADN fongique (génétique)</term>
<term>Cartographie de restriction (MeSH)</term>
<term>Chrysosporium (enzymologie)</term>
<term>Chrysosporium (génétique)</term>
<term>Clones cellulaires (analyse)</term>
<term>Deuteromycota (génétique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Gènes (MeSH)</term>
<term>Oxygénases (génétique)</term>
<term>Séquence nucléotidique (MeSH)</term>
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<term>DNA</term>
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<term>ADN</term>
<term>Clones cellulaires</term>
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<keywords scheme="MESH" qualifier="analysis" xml:lang="en">
<term>Clone Cells</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Chrysosporium</term>
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<term>Chrysosporium</term>
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<term>Chrysosporium</term>
<term>DNA, Fungal</term>
<term>Mitosporic Fungi</term>
<term>Oxygenases</term>
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<term>Deuteromycota</term>
<term>Oxygénases</term>
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<term>Base Sequence</term>
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<term>Molecular Sequence Data</term>
<term>Restriction Mapping</term>
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<term>Cartographie de restriction</term>
<term>Données de séquences moléculaires</term>
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<div type="abstract" xml:lang="en">The basidiomycete fungus Phanerochaete chrysosporium produces a number of extracellular peroxidases which appear to be important for lignin degradation. We present here the isolation and complete nucleotide (nt) sequence of a gene (lpo) coding for lignin peroxidase (LPO), the coding region of which is identical to a lpo cDNA sequence which had previously been described [M. Tien and C.-P.D. Tu, Nature 326 (1987) 520-523]. The deduced amino acid (aa) sequence corresponds to 372 aa residues and the coding region is interrupted by eight short introns that range in size from 50 to 62 nt. Southern blot experiments using the cloned lpo gene as hybridization probe revealed a complex restriction fragment pattern, indicating that there are a number of lpo-related nucleotide sequences present in P. chrysosporium DNA which cross-hybridize. We also present data on the in vivo expression of the lpo genes and show that they are regulated at the RNA level and that the structure of the transcripts as judged from S1 experiments is complex. These data are consistent with the idea that there are a number of related lpo genes in P. chrysosporium which constitute a gene family.</div>
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<AbstractText>The basidiomycete fungus Phanerochaete chrysosporium produces a number of extracellular peroxidases which appear to be important for lignin degradation. We present here the isolation and complete nucleotide (nt) sequence of a gene (lpo) coding for lignin peroxidase (LPO), the coding region of which is identical to a lpo cDNA sequence which had previously been described [M. Tien and C.-P.D. Tu, Nature 326 (1987) 520-523]. The deduced amino acid (aa) sequence corresponds to 372 aa residues and the coding region is interrupted by eight short introns that range in size from 50 to 62 nt. Southern blot experiments using the cloned lpo gene as hybridization probe revealed a complex restriction fragment pattern, indicating that there are a number of lpo-related nucleotide sequences present in P. chrysosporium DNA which cross-hybridize. We also present data on the in vivo expression of the lpo genes and show that they are regulated at the RNA level and that the structure of the transcripts as judged from S1 experiments is complex. These data are consistent with the idea that there are a number of related lpo genes in P. chrysosporium which constitute a gene family.</AbstractText>
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