PhanerochaeteV1, Main, Curation, bibRecord, 000861

A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member.

Identifieur interne : 000861 ( Main/Curation ); précédent : 000860; suivant : 000862

A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member.

Auteurs : Vincenza Faraco [Italie] ; Gianna Palmieri [Italie] ; Giovanna Festa [Italie] ; Maria Monti [Italie] ; Giovanni Sannia [Italie] ; Paola Giardina [Italie]

Source :

Microbiology (Reading, England) [ 1350-0872 ] ; 2005.

RBID : pubmed:15699195

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Fungal (MeSH), Molecular Sequence Data (MeSH), Peptide Hydrolases (genetics), Peptide Hydrolases (metabolism), Pleurotus (enzymology), Pleurotus (genetics), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Structure-Activity Relationship (MeSH), Substrate Specificity (MeSH), Subtilisins (chemistry), Subtilisins (genetics), Subtilisins (metabolism).
MESH :
- chemical , chemistry : Subtilisins.
- chemical , genetics : Fungal Proteins, Peptide Hydrolases, Subtilisins.
- chemical , metabolism : Fungal Proteins, Peptide Hydrolases, Subtilisins.
- chemical : DNA, Complementary.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- Amino Acid Sequence, Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Molecular Sequence Data, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Structure-Activity Relationship, Substrate Specificity.

Abstract

Pleurotus ostreatus produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant P. ostreatus extracellular protease (PoSl) have been reported. The sequence of the posl gene and of the corresponding cDNA has been determined, allowing the identification of its pre- and pro-sequences. A mature protein sequence has been verified by mass spectrometry mapping, the N-glycosylation sites have been identified and the glycosidic moieties characterized. Mature PoSl shows a cleaved peptide bond in the C-terminal region, which remains associated with the catalytic domain in a non-covalent complex. Reported results indicate that this enzyme is involved in the activation of other P. ostreatus secreted proteases, thus suggesting its leading role in cascade activation mechanisms. Analyses of the PoSl sequence by homology search resulted in the identification of a DNA sequence encoding a new protease, homologous to PoSl, in the Phanerochaete chrysosporium genome. A new subgroup of subtilisin-like proteases, belonging to the pyrolysin family, has been defined, which includes proteases from ascomycete and basidiomycete fungi.

DOI: 10.1099/mic.0.27441-0
PubMed: 15699195

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

to stream Main, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000861

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pubmed:15699195

Le document en format XML

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<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression Regulation, Enzymologic (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
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<term>Peptide Hydrolases (metabolism)</term>
<term>Pleurotus (enzymology)</term>
<term>Pleurotus (genetics)</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
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<term>Subtilisins (genetics)</term>
<term>Subtilisins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Peptide hydrolases (génétique)</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Pleurotus (enzymologie)</term>
<term>Pleurotus (génétique)</term>
<term>Protéines fongiques (génétique)</term>
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<term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Spectrométrie de masse MALDI (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Subtilisines (composition chimique)</term>
<term>Subtilisines (génétique)</term>
<term>Subtilisines (métabolisme)</term>
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<term>Molecular Sequence Data</term>
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<term>Régulation de l'expression des gènes fongiques</term>
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<front><div type="abstract" xml:lang="en">Pleurotus ostreatus produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant P. ostreatus extracellular protease (PoSl) have been reported. The sequence of the posl gene and of the corresponding cDNA has been determined, allowing the identification of its pre- and pro-sequences. A mature protein sequence has been verified by mass spectrometry mapping, the N-glycosylation sites have been identified and the glycosidic moieties characterized. Mature PoSl shows a cleaved peptide bond in the C-terminal region, which remains associated with the catalytic domain in a non-covalent complex. Reported results indicate that this enzyme is involved in the activation of other P. ostreatus secreted proteases, thus suggesting its leading role in cascade activation mechanisms. Analyses of the PoSl sequence by homology search resulted in the identification of a DNA sequence encoding a new protease, homologous to PoSl, in the Phanerochaete chrysosporium genome. A new subgroup of subtilisin-like proteases, belonging to the pyrolysin family, has been defined, which includes proteases from ascomycete and basidiomycete fungi.</div>
</front>
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<DateCompleted><Year>2005</Year>
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<Month>Feb</Month>
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<Title>Microbiology (Reading, England)</Title>
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<ArticleTitle>A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member.</ArticleTitle>
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<Abstract><AbstractText>Pleurotus ostreatus produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant P. ostreatus extracellular protease (PoSl) have been reported. The sequence of the posl gene and of the corresponding cDNA has been determined, allowing the identification of its pre- and pro-sequences. A mature protein sequence has been verified by mass spectrometry mapping, the N-glycosylation sites have been identified and the glycosidic moieties characterized. Mature PoSl shows a cleaved peptide bond in the C-terminal region, which remains associated with the catalytic domain in a non-covalent complex. Reported results indicate that this enzyme is involved in the activation of other P. ostreatus secreted proteases, thus suggesting its leading role in cascade activation mechanisms. Analyses of the PoSl sequence by homology search resulted in the identification of a DNA sequence encoding a new protease, homologous to PoSl, in the Phanerochaete chrysosporium genome. A new subgroup of subtilisin-like proteases, belonging to the pyrolysin family, has been defined, which includes proteases from ascomycete and basidiomycete fungi.</AbstractText>
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<ForeName>Vincenza</ForeName>
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</AffiliationInfo>
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<ForeName>Gianna</ForeName>
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<AffiliationInfo><Affiliation>ISPAAM, Consiglio Nazionale delle Ricerche, via Argine 1085, 80147 Napoli, Italy.</Affiliation>
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<Author ValidYN="Y"><LastName>Festa</LastName>
<ForeName>Giovanna</ForeName>
<Initials>G</Initials>
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<Author ValidYN="Y"><LastName>Monti</LastName>
<ForeName>Maria</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Dipartimento di Chimica Organica e Biochimica, Università di Napoli 'Federico II', Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Napoli, Italy.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Sannia</LastName>
<ForeName>Giovanni</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Dipartimento di Chimica Organica e Biochimica, Università di Napoli 'Federico II', Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Napoli, Italy.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Giardina</LastName>
<ForeName>Paola</ForeName>
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A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member.

A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member.

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