PhanerochaeteV1, Main, Exploration, bibRecord, 000698

Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation.

Identifieur interne : 000698 ( Main/Exploration ); précédent : 000697; suivant : 000699

Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation.

Auteurs : Semarjit Shary [États-Unis] ; Alexander N. Kapich ; Ellen A. Panisko ; Jon K. Magnuson ; Daniel Cullen ; Kenneth E. Hammel

Source :

Applied and environmental microbiology [ 1098-5336 ] ; 2008.

RBID : pubmed:18849459

Descripteurs français

English descriptors

KwdEn :
- Carbon Radioisotopes (metabolism), Cellulose (metabolism), Chromatography, Liquid (MeSH), Enzymes (biosynthesis), Fungal Proteins (biosynthesis), Gene Expression Profiling (MeSH), Glucose (metabolism), Intracellular Membranes (chemistry), Lignin (metabolism), Membrane Proteins (biosynthesis), Membrane Transport Proteins (biosynthesis), Microsomes (chemistry), Phanerochaete (chemistry), Phanerochaete (metabolism), Tandem Mass Spectrometry (MeSH).
MESH :
- chemical , biosynthesis : Enzymes, Fungal Proteins, Membrane Proteins, Membrane Transport Proteins.
- chemical , metabolism : Carbon Radioisotopes, Cellulose, Glucose, Lignin.
- chemistry : Intracellular Membranes, Microsomes, Phanerochaete.
- metabolism : Phanerochaete.
- Chromatography, Liquid, Gene Expression Profiling, Tandem Mass Spectrometry.

Abstract

Fungal lignin-degrading systems likely include membrane-associated proteins that participate in diverse processes such as uptake and oxidation of lignin fragments, production of ligninolytic secondary metabolites, and defense of the mycelium against ligninolytic oxidants. Little is known about the nature or regulation of these membrane-associated components. We grew the white rot basidiomycete Phanerochaete chrysosporium on cellulose or glucose as the carbon source and monitored the mineralization of a (14)C-labeled synthetic lignin by these cultures to assess their ligninolytic competence. The results showed that the cellulose-grown cultures were ligninolytic, whereas the glucose-grown ones were not. We isolated microsomal membrane fractions from both types of culture and analyzed tryptic digests of their proteins by shotgun liquid chromatography-tandem mass spectrometry. Comparison of the results against the predicted P. chrysosporium proteome showed that a catalase (Joint Genome Institute P. chrysosporium protein identification number [I.D.] 124398), an alcohol oxidase (126879), two transporters (137220 and 132234), and two cytochrome P450s (5011 and 8912) were upregulated under ligninolytic conditions. Quantitative reverse transcription-PCR assays showed that RNA transcripts encoding all of these proteins were also more abundant in ligninolytic cultures. Catalase 124398, alcohol oxidase 126879, and transporter 137220 were found in a proteomic analysis of partially purified plasma membranes from ligninolytic P. chrysosporium and are therefore most likely associated with the outer envelope of the fungus.

DOI: 10.1128/AEM.01997-08
PubMed: 18849459
PubMed Central: PMC2592923

Affiliations:

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Le document en format XML

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<term>Enzymes (biosynthesis)</term>
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<term>Enzymes (biosynthèse)</term>
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<term>Lignine (métabolisme)</term>
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<term>Protéines fongiques (biosynthèse)</term>
<term>Protéines membranaires (biosynthèse)</term>
<term>Radio-isotopes du carbone (métabolisme)</term>
<term>Spectrométrie de masse en tandem (MeSH)</term>
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<term>Fungal Proteins</term>
<term>Membrane Proteins</term>
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<term>Protéines membranaires</term>
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<term>Phanerochaete</term>
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<front><div type="abstract" xml:lang="en">Fungal lignin-degrading systems likely include membrane-associated proteins that participate in diverse processes such as uptake and oxidation of lignin fragments, production of ligninolytic secondary metabolites, and defense of the mycelium against ligninolytic oxidants. Little is known about the nature or regulation of these membrane-associated components. We grew the white rot basidiomycete Phanerochaete chrysosporium on cellulose or glucose as the carbon source and monitored the mineralization of a (14)C-labeled synthetic lignin by these cultures to assess their ligninolytic competence. The results showed that the cellulose-grown cultures were ligninolytic, whereas the glucose-grown ones were not. We isolated microsomal membrane fractions from both types of culture and analyzed tryptic digests of their proteins by shotgun liquid chromatography-tandem mass spectrometry. Comparison of the results against the predicted P. chrysosporium proteome showed that a catalase (Joint Genome Institute P. chrysosporium protein identification number [I.D.] 124398), an alcohol oxidase (126879), two transporters (137220 and 132234), and two cytochrome P450s (5011 and 8912) were upregulated under ligninolytic conditions. Quantitative reverse transcription-PCR assays showed that RNA transcripts encoding all of these proteins were also more abundant in ligninolytic cultures. Catalase 124398, alcohol oxidase 126879, and transporter 137220 were found in a proteomic analysis of partially purified plasma membranes from ligninolytic P. chrysosporium and are therefore most likely associated with the outer envelope of the fungus.</div>
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<Abstract><AbstractText>Fungal lignin-degrading systems likely include membrane-associated proteins that participate in diverse processes such as uptake and oxidation of lignin fragments, production of ligninolytic secondary metabolites, and defense of the mycelium against ligninolytic oxidants. Little is known about the nature or regulation of these membrane-associated components. We grew the white rot basidiomycete Phanerochaete chrysosporium on cellulose or glucose as the carbon source and monitored the mineralization of a (14)C-labeled synthetic lignin by these cultures to assess their ligninolytic competence. The results showed that the cellulose-grown cultures were ligninolytic, whereas the glucose-grown ones were not. We isolated microsomal membrane fractions from both types of culture and analyzed tryptic digests of their proteins by shotgun liquid chromatography-tandem mass spectrometry. Comparison of the results against the predicted P. chrysosporium proteome showed that a catalase (Joint Genome Institute P. chrysosporium protein identification number [I.D.] 124398), an alcohol oxidase (126879), two transporters (137220 and 132234), and two cytochrome P450s (5011 and 8912) were upregulated under ligninolytic conditions. Quantitative reverse transcription-PCR assays showed that RNA transcripts encoding all of these proteins were also more abundant in ligninolytic cultures. Catalase 124398, alcohol oxidase 126879, and transporter 137220 were found in a proteomic analysis of partially purified plasma membranes from ligninolytic P. chrysosporium and are therefore most likely associated with the outer envelope of the fungus.</AbstractText>
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   |texte=   Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation.
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Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation.

Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation.

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