PhanerochaeteV1, Main, Exploration, bibRecord, 000297

Study of Phanerochaete chrysosporium secretome revealed protein glycosylation as a substrate-dependent post-translational modification.

Identifieur interne : 000297 ( Main/Exploration ); précédent : 000296; suivant : 000298

Study of Phanerochaete chrysosporium secretome revealed protein glycosylation as a substrate-dependent post-translational modification.

Auteurs : Sunil S. Adav ; Anita Ravindran ; Siu Kwan Sze

Source :

Journal of proteome research [ 1535-3907 ] ; 2014.

RBID : pubmed:25162795

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Chromatography, Liquid (MeSH), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Glycoproteins (chemistry), Glycoproteins (metabolism), Glycosylation (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (metabolism), Protein Processing, Post-Translational (MeSH), Tandem Mass Spectrometry (MeSH).
MESH :
- chemical , chemistry : Fungal Proteins, Glycoproteins.
- chemical , metabolism : Fungal Proteins, Glycoproteins.
- metabolism : Phanerochaete.
- Amino Acid Sequence, Chromatography, Liquid, Glycosylation, Molecular Sequence Data, Protein Processing, Post-Translational, Tandem Mass Spectrometry.

Abstract

Lignocellulosic biomass is a potential sustainable resource of mixed sugars that can be exploited for biofuel and other biomaterials. Phanerochaete chrysosporium (P. chrysosporium) produce an arsenal of extracellular enzymes, the secretome, for efficiently degrading lignocellulosic biomass. Post-translational modifications (PTMs) of these biomass-degrading enzymes generate remarkable diversity, complexity, heterogeneity and also alter physiological behavior, function, and activities. Identification of PTMs and the sites of modifications of these secreted proteins remain as an essential but unexploited step to understand the biomass degradation mechanism. Therefore, this study applied electrostatic repulsion hydrophilic interaction chromatography (ERLIC) for glycopeptides enrichment and coupled with tandem mass spectrometry (LC-MS/MS) analysis for glycosylated secreted enzymes of P. chrysosporium during glucose, cellulose, and lignin degradation. Varied groups of enzymes, including cellulases, glycoside hydrolases, hemicellulases, lignin-degrading enzymes, were glycosylated. The comparisons of the glycosylated secreted enzymes of P. chrysosporium in glucose, cellulose, and lignin culture conditions revealed glycosylation as substrate-dependent PTMs.

DOI: 10.1021/pr500385y
PubMed: 25162795

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Chromatography, Liquid (MeSH)</term>
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<term>Fungal Proteins (metabolism)</term>
<term>Glycoproteins (chemistry)</term>
<term>Glycoproteins (metabolism)</term>
<term>Glycosylation (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phanerochaete (metabolism)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Tandem Mass Spectrometry (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie en phase liquide (MeSH)</term>
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<term>Glycoprotéines (composition chimique)</term>
<term>Glycoprotéines (métabolisme)</term>
<term>Glycosylation (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Phanerochaete (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Spectrométrie de masse en tandem (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term>
<term>Glycoproteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycoprotéines</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Chromatography, Liquid</term>
<term>Glycosylation</term>
<term>Molecular Sequence Data</term>
<term>Protein Processing, Post-Translational</term>
<term>Tandem Mass Spectrometry</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide</term>
<term>Données de séquences moléculaires</term>
<term>Glycosylation</term>
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<front><div type="abstract" xml:lang="en">Lignocellulosic biomass is a potential sustainable resource of mixed sugars that can be exploited for biofuel and other biomaterials. Phanerochaete chrysosporium (P. chrysosporium) produce an arsenal of extracellular enzymes, the secretome, for efficiently degrading lignocellulosic biomass. Post-translational modifications (PTMs) of these biomass-degrading enzymes generate remarkable diversity, complexity, heterogeneity and also alter physiological behavior, function, and activities. Identification of PTMs and the sites of modifications of these secreted proteins remain as an essential but unexploited step to understand the biomass degradation mechanism. Therefore, this study applied electrostatic repulsion hydrophilic interaction chromatography (ERLIC) for glycopeptides enrichment and coupled with tandem mass spectrometry (LC-MS/MS) analysis for glycosylated secreted enzymes of P. chrysosporium during glucose, cellulose, and lignin degradation. Varied groups of enzymes, including cellulases, glycoside hydrolases, hemicellulases, lignin-degrading enzymes, were glycosylated. The comparisons of the glycosylated secreted enzymes of P. chrysosporium in glucose, cellulose, and lignin culture conditions revealed glycosylation as substrate-dependent PTMs. </div>
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Study of Phanerochaete chrysosporium secretome revealed protein glycosylation as a substrate-dependent post-translational modification.

Study of Phanerochaete chrysosporium secretome revealed protein glycosylation as a substrate-dependent post-translational modification.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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