GlutaredoxinV1, Main, Exploration, bibRecord, 000B63

The machinery for oxidative protein folding in thermophiles.

Identifieur interne : 000B63 ( Main/Exploration ); précédent : 000B62; suivant : 000B64

The machinery for oxidative protein folding in thermophiles.

Auteurs : Emilia Pedone [Italie] ; Danila Limauro ; Simonetta Bartolucci

Source :

Antioxidants & redox signaling [ 1523-0864 ] ; 2008.

RBID : pubmed:17956189

Descripteurs français

KwdFr :
- Bactéries (enzymologie), Catalyse (MeSH), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Pliage des protéines (MeSH), Protein Disulfide-Isomerases (composition chimique), Protein Disulfide-Isomerases (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
MESH :
- composition chimique : Glutarédoxines, Protein Disulfide-Isomerases, Thiorédoxines.
- enzymologie : Bactéries.
- métabolisme : Disulfures, Glutarédoxines, Protein Disulfide-Isomerases, Thiorédoxines.
- Catalyse, Données de séquences moléculaires, Modèles moléculaires, Oxydoréduction, Pliage des protéines, Similitude de séquences d'acides aminés, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Bacteria (enzymology), Catalysis (MeSH), Disulfides (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Protein Disulfide-Isomerases (chemistry), Protein Disulfide-Isomerases (metabolism), Protein Folding (MeSH), Sequence Homology, Amino Acid (MeSH), Thioredoxins (chemistry), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Glutaredoxins, Protein Disulfide-Isomerases, Thioredoxins.
- chemical , metabolism : Disulfides, Glutaredoxins, Protein Disulfide-Isomerases, Thioredoxins.
- enzymology : Bacteria.
- Amino Acid Sequence, Catalysis, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Folding, Sequence Homology, Amino Acid.

Abstract

Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts.

DOI: 10.1089/ars.2007.1855
PubMed: 17956189

Affiliations:

Italie

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

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Le document en format XML

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<author><name sortKey="Pedone, Emilia" sort="Pedone, Emilia" uniqKey="Pedone E" first="Emilia" last="Pedone">Emilia Pedone</name>
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<author><name sortKey="Limauro, Danila" sort="Limauro, Danila" uniqKey="Limauro D" first="Danila" last="Limauro">Danila Limauro</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Bacteria (enzymology)</term>
<term>Catalysis (MeSH)</term>
<term>Disulfides (metabolism)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Disulfide-Isomerases (chemistry)</term>
<term>Protein Disulfide-Isomerases (metabolism)</term>
<term>Protein Folding (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Thioredoxins (chemistry)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Bactéries (enzymologie)</term>
<term>Catalyse (MeSH)</term>
<term>Disulfures (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Protein Disulfide-Isomerases (composition chimique)</term>
<term>Protein Disulfide-Isomerases (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thiorédoxines (composition chimique)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Protein Disulfide-Isomerases</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term>
<term>Glutaredoxins</term>
<term>Protein Disulfide-Isomerases</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protein Disulfide-Isomerases</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactéries</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteria</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term>
<term>Glutarédoxines</term>
<term>Protein Disulfide-Isomerases</term>
<term>Thiorédoxines</term>
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<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Oxidation-Reduction</term>
<term>Protein Folding</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Oxydoréduction</term>
<term>Pliage des protéines</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts.</div>
</front>
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<DateRevised><Year>2008</Year>
<Month>11</Month>
<Day>21</Day>
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<Issue>1</Issue>
<PubDate><Year>2008</Year>
<Month>Jan</Month>
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<Title>Antioxidants & redox signaling</Title>
<ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation>
</Journal>
<ArticleTitle>The machinery for oxidative protein folding in thermophiles.</ArticleTitle>
<Pagination><MedlinePgn>157-69</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts.</AbstractText>
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The machinery for oxidative protein folding in thermophiles.

The machinery for oxidative protein folding in thermophiles.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki