GlutaredoxinV1, Main, Exploration, bibRecord, 000E75

Identification of a redox-regulated chaperone network.

Identifieur interne : 000E75 ( Main/Exploration ); précédent : 000E74; suivant : 000E76

Identification of a redox-regulated chaperone network.

Auteurs : Jörg H. Hoffmann [États-Unis] ; Katrin Linke ; Paul C F. Graf ; Hauke Lilie ; Ursula Jakob

Source :

The EMBO journal [ 0261-4189 ] ; 2004.

RBID : pubmed:14685279

Descripteurs français

KwdFr :
- Animaux (MeSH), Bovins (MeSH), Chaperons moléculaires (composition chimique), Chaperons moléculaires (génétique), Chaperons moléculaires (métabolisme), Chaperons moléculaires (physiologie), Citrate (si)-synthase (métabolisme), Conformation des protéines (MeSH), Cystéine (composition chimique), Dimérisation (MeSH), Disulfures (composition chimique), Dithiothréitol (pharmacologie), Dénaturation des protéines (MeSH), Facteurs temps (MeSH), Luciferases (métabolisme), Maturation post-traductionnelle des protéines (MeSH), Modèles biologiques (MeSH), Oxydoréduction (MeSH), Pliage des protéines (MeSH), Polarisation de fluorescence (MeSH), Protéines du choc thermique (composition chimique), Protéines du choc thermique (génétique), Protéines du choc thermique (métabolisme), Protéines du choc thermique (physiologie), Réducteurs (pharmacologie), Spécificité du substrat (MeSH), Suidae (MeSH), Sérumalbumine bovine (métabolisme), Température (MeSH).
MESH :
- composition chimique : Chaperons moléculaires, Cystéine, Disulfures, Protéines du choc thermique.
- génétique : Chaperons moléculaires, Protéines du choc thermique.
- métabolisme : Chaperons moléculaires, Citrate (si)-synthase, Luciferases, Protéines du choc thermique, Sérumalbumine bovine.
- pharmacologie : Dithiothréitol, Réducteurs.
- physiologie : Chaperons moléculaires, Protéines du choc thermique.
- Animaux, Bovins, Conformation des protéines, Dimérisation, Dénaturation des protéines, Facteurs temps, Maturation post-traductionnelle des protéines, Modèles biologiques, Oxydoréduction, Pliage des protéines, Polarisation de fluorescence, Spécificité du substrat, Suidae, Température.

English descriptors

KwdEn :
- Animals (MeSH), Cattle (MeSH), Citrate (si)-Synthase (metabolism), Cysteine (chemistry), Dimerization (MeSH), Disulfides (chemistry), Dithiothreitol (pharmacology), Fluorescence Polarization (MeSH), Heat-Shock Proteins (chemistry), Heat-Shock Proteins (genetics), Heat-Shock Proteins (metabolism), Heat-Shock Proteins (physiology), Luciferases (metabolism), Models, Biological (MeSH), Molecular Chaperones (chemistry), Molecular Chaperones (genetics), Molecular Chaperones (metabolism), Molecular Chaperones (physiology), Oxidation-Reduction (MeSH), Protein Conformation (MeSH), Protein Denaturation (MeSH), Protein Folding (MeSH), Protein Processing, Post-Translational (MeSH), Reducing Agents (pharmacology), Serum Albumin, Bovine (metabolism), Substrate Specificity (MeSH), Swine (MeSH), Temperature (MeSH), Time Factors (MeSH).
MESH :
- chemical , chemistry : Cysteine, Disulfides, Heat-Shock Proteins, Molecular Chaperones.
- chemical , genetics : Heat-Shock Proteins, Molecular Chaperones.
- chemical , metabolism : Citrate (si)-Synthase, Heat-Shock Proteins, Luciferases, Molecular Chaperones, Serum Albumin, Bovine.
- chemical , pharmacology : Dithiothreitol, Reducing Agents.
- chemical , physiology : Heat-Shock Proteins, Molecular Chaperones.
- Animals, Cattle, Dimerization, Fluorescence Polarization, Models, Biological, Oxidation-Reduction, Protein Conformation, Protein Denaturation, Protein Folding, Protein Processing, Post-Translational, Substrate Specificity, Swine, Temperature, Time Factors.

Abstract

We have identified and reconstituted a multicomponent redox-chaperone network that appears to be designed to protect proteins against stress-induced unfolding and to refold proteins when conditions return to normal. The central player is Hsp33, a redox-regulated molecular chaperone. Hsp33, which is activated by disulfide bond formation and subsequent dimerization, works as an efficient chaperone holdase that binds to unfolding protein intermediates and maintains them in a folding competent conformation. Reduction of Hsp33 is catalyzed by the glutaredoxin and thioredoxin systems in vivo, and leads to the formation of highly active, reduced Hsp33 dimers. Reduction of Hsp33 is necessary but not sufficient for substrate protein release. Substrate dissociation from Hsp33 is linked to the presence of the DnaK/DnaJ/GrpE foldase system, which alone, or in concert with the GroEL/GroES system, then supports the refolding of the substrate proteins. Upon substrate release, reduced Hsp33 dimers dissociate into inactive monomers. This regulated substrate transfer ultimately links substrate release and Hsp33 inactivation to the presence of available DnaK/DnaJ/GrpE, and, therefore, to the return of cells to non-stress conditions.

DOI: 10.1038/sj.emboj.7600016
PubMed: 14685279
PubMed Central: PMC1271656

Affiliations:

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

to stream Main, to step Corpus: 000E94
to stream Main, to step Curation: 000E94

Le document en format XML

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<term>Cattle (MeSH)</term>
<term>Citrate (si)-Synthase (metabolism)</term>
<term>Cysteine (chemistry)</term>
<term>Dimerization (MeSH)</term>
<term>Disulfides (chemistry)</term>
<term>Dithiothreitol (pharmacology)</term>
<term>Fluorescence Polarization (MeSH)</term>
<term>Heat-Shock Proteins (chemistry)</term>
<term>Heat-Shock Proteins (genetics)</term>
<term>Heat-Shock Proteins (metabolism)</term>
<term>Heat-Shock Proteins (physiology)</term>
<term>Luciferases (metabolism)</term>
<term>Models, Biological (MeSH)</term>
<term>Molecular Chaperones (chemistry)</term>
<term>Molecular Chaperones (genetics)</term>
<term>Molecular Chaperones (metabolism)</term>
<term>Molecular Chaperones (physiology)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Denaturation (MeSH)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Reducing Agents (pharmacology)</term>
<term>Serum Albumin, Bovine (metabolism)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Swine (MeSH)</term>
<term>Temperature (MeSH)</term>
<term>Time Factors (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Bovins (MeSH)</term>
<term>Chaperons moléculaires (composition chimique)</term>
<term>Chaperons moléculaires (génétique)</term>
<term>Chaperons moléculaires (métabolisme)</term>
<term>Chaperons moléculaires (physiologie)</term>
<term>Citrate (si)-synthase (métabolisme)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cystéine (composition chimique)</term>
<term>Dimérisation (MeSH)</term>
<term>Disulfures (composition chimique)</term>
<term>Dithiothréitol (pharmacologie)</term>
<term>Dénaturation des protéines (MeSH)</term>
<term>Facteurs temps (MeSH)</term>
<term>Luciferases (métabolisme)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Polarisation de fluorescence (MeSH)</term>
<term>Protéines du choc thermique (composition chimique)</term>
<term>Protéines du choc thermique (génétique)</term>
<term>Protéines du choc thermique (métabolisme)</term>
<term>Protéines du choc thermique (physiologie)</term>
<term>Réducteurs (pharmacologie)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Suidae (MeSH)</term>
<term>Sérumalbumine bovine (métabolisme)</term>
<term>Température (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term>
<term>Disulfides</term>
<term>Heat-Shock Proteins</term>
<term>Molecular Chaperones</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Heat-Shock Proteins</term>
<term>Molecular Chaperones</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Citrate (si)-Synthase</term>
<term>Heat-Shock Proteins</term>
<term>Luciferases</term>
<term>Molecular Chaperones</term>
<term>Serum Albumin, Bovine</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Dithiothreitol</term>
<term>Reducing Agents</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Heat-Shock Proteins</term>
<term>Molecular Chaperones</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Chaperons moléculaires</term>
<term>Cystéine</term>
<term>Disulfures</term>
<term>Protéines du choc thermique</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chaperons moléculaires</term>
<term>Protéines du choc thermique</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chaperons moléculaires</term>
<term>Citrate (si)-synthase</term>
<term>Luciferases</term>
<term>Protéines du choc thermique</term>
<term>Sérumalbumine bovine</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Dithiothréitol</term>
<term>Réducteurs</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Chaperons moléculaires</term>
<term>Protéines du choc thermique</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cattle</term>
<term>Dimerization</term>
<term>Fluorescence Polarization</term>
<term>Models, Biological</term>
<term>Oxidation-Reduction</term>
<term>Protein Conformation</term>
<term>Protein Denaturation</term>
<term>Protein Folding</term>
<term>Protein Processing, Post-Translational</term>
<term>Substrate Specificity</term>
<term>Swine</term>
<term>Temperature</term>
<term>Time Factors</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Bovins</term>
<term>Conformation des protéines</term>
<term>Dimérisation</term>
<term>Dénaturation des protéines</term>
<term>Facteurs temps</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Modèles biologiques</term>
<term>Oxydoréduction</term>
<term>Pliage des protéines</term>
<term>Polarisation de fluorescence</term>
<term>Spécificité du substrat</term>
<term>Suidae</term>
<term>Température</term>
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<front><div type="abstract" xml:lang="en">We have identified and reconstituted a multicomponent redox-chaperone network that appears to be designed to protect proteins against stress-induced unfolding and to refold proteins when conditions return to normal. The central player is Hsp33, a redox-regulated molecular chaperone. Hsp33, which is activated by disulfide bond formation and subsequent dimerization, works as an efficient chaperone holdase that binds to unfolding protein intermediates and maintains them in a folding competent conformation. Reduction of Hsp33 is catalyzed by the glutaredoxin and thioredoxin systems in vivo, and leads to the formation of highly active, reduced Hsp33 dimers. Reduction of Hsp33 is necessary but not sufficient for substrate protein release. Substrate dissociation from Hsp33 is linked to the presence of the DnaK/DnaJ/GrpE foldase system, which alone, or in concert with the GroEL/GroES system, then supports the refolding of the substrate proteins. Upon substrate release, reduced Hsp33 dimers dissociate into inactive monomers. This regulated substrate transfer ultimately links substrate release and Hsp33 inactivation to the presence of available DnaK/DnaJ/GrpE, and, therefore, to the return of cells to non-stress conditions.</div>
</front>
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<Abstract><AbstractText>We have identified and reconstituted a multicomponent redox-chaperone network that appears to be designed to protect proteins against stress-induced unfolding and to refold proteins when conditions return to normal. The central player is Hsp33, a redox-regulated molecular chaperone. Hsp33, which is activated by disulfide bond formation and subsequent dimerization, works as an efficient chaperone holdase that binds to unfolding protein intermediates and maintains them in a folding competent conformation. Reduction of Hsp33 is catalyzed by the glutaredoxin and thioredoxin systems in vivo, and leads to the formation of highly active, reduced Hsp33 dimers. Reduction of Hsp33 is necessary but not sufficient for substrate protein release. Substrate dissociation from Hsp33 is linked to the presence of the DnaK/DnaJ/GrpE foldase system, which alone, or in concert with the GroEL/GroES system, then supports the refolding of the substrate proteins. Upon substrate release, reduced Hsp33 dimers dissociate into inactive monomers. This regulated substrate transfer ultimately links substrate release and Hsp33 inactivation to the presence of available DnaK/DnaJ/GrpE, and, therefore, to the return of cells to non-stress conditions.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hoffmann</LastName>
<ForeName>Jörg H</ForeName>
<Initials>JH</Initials>
<AffiliationInfo><Affiliation>Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Graf</LastName>
<ForeName>Paul C F</ForeName>
<Initials>PC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lilie</LastName>
<ForeName>Hauke</ForeName>
<Initials>H</Initials>
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<Author ValidYN="Y"><LastName>Jakob</LastName>
<ForeName>Ursula</ForeName>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002950" MajorTopicYN="N">Citrate (si)-Synthase</DescriptorName>
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<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName>
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<MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
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<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="Y">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019163" MajorTopicYN="N">Reducing Agents</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012710" MajorTopicYN="N">Serum Albumin, Bovine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2003</Year>
<Month>05</Month>
<Day>27</Day>
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Identification of a redox-regulated chaperone network.

Identification of a redox-regulated chaperone network.

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