MersV1, Main, Exploration, bibRecordById, pubmed:1680127

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

Identifieur interne : 004873 ( Main/Exploration ); précédent : 004872; suivant : 004874

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

Auteurs : J A Mendoza ; G H Lorimer ; P M Horowitz

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 1991.

RBID : pubmed:1680127

Descripteurs français

KwdFr :
- Adénosine triphosphate (métabolisme), Chaperonine-60, Chaperonines, Cinétique, Conformation des protéines, Protéines (), Protéines bactériennes (), Protéines du choc thermique (), Température, Thiosulfate sulfurtransferase (), Urée.
MESH :
- métabolisme : Adénosine triphosphate.
- Chaperonine-60, Chaperonines, Cinétique, Conformation des protéines, Protéines, Protéines bactériennes, Protéines du choc thermique, Température, Thiosulfate sulfurtransferase, Urée.

English descriptors

KwdEn :
- Adenosine Triphosphate (metabolism), Bacterial Proteins (chemistry), Chaperonin 60, Chaperonins, Heat-Shock Proteins (chemistry), Kinetics, Protein Conformation, Proteins (chemistry), Temperature, Thiosulfate Sulfurtransferase (chemistry), Urea.
MESH :
- chemical , chemistry : Bacterial Proteins, Heat-Shock Proteins, Proteins, Thiosulfate Sulfurtransferase.
- chemical , metabolism : Adenosine Triphosphate.
- chemical : Chaperonin 60, Chaperonins, Urea.
- Kinetics, Protein Conformation, Temperature.

Abstract

In vitro refolding of the urea-unfolded, monomeric, mitochondrial enzyme rhodanese (thiosulfate sulfur-transferase; EC 2.8.1.1) is facilitated by the chaperonin proteins cpn60 and cpn10 from Escherichia coli at 37 degrees C, but the refolding is strongly inhibited at 10 degrees C. In contrast, the unassisted refolding of rhodanese is efficient at 10 degrees C, but the refolding efficiency decreases as the temperature is raised. These observations provided two measures of the cpn60-rhodanese complex. Thus, we monitored either 1) the cpn60-dependent inhibition of spontaneous folding at 10 degrees C or 2) the recovery of active rhodanese in the complete chaperonin system at 25 degrees C, after first forming a cpn60-rhodanese complex at 10 degrees C. These procedures minimized the aggregation of interactive folding intermediates that tend to overestimate the apparent number of cpn60 14-mers in determining the stoichiometry of protein-cpn60 14-mer interactions. Both procedures used here gave results that were consistent with there being 1 rhodanese binding site/cpn60 tetradecamer. This stoichiometry is significantly less than might be expected from the fact that cpn60 is composed of 14 identical subunits, and it may indicate that rhodanese interacts with a restricted region that is formed when the cpn60 tetradecamer is assembled. The ability to stabilize chaperonin-protein complexes that can subsequently be reactivated will aid studies of the mode of action of the ubiquitous chaperonin proteins.

PubMed: 1680127

Affiliations:

Le document en format XML

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<term>Chaperonins</term>
<term>Heat-Shock Proteins (chemistry)</term>
<term>Kinetics</term>
<term>Protein Conformation</term>
<term>Proteins (chemistry)</term>
<term>Temperature</term>
<term>Thiosulfate Sulfurtransferase (chemistry)</term>
<term>Urea</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Adénosine triphosphate (métabolisme)</term>
<term>Chaperonine-60</term>
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<term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Protéines ()</term>
<term>Protéines bactériennes ()</term>
<term>Protéines du choc thermique ()</term>
<term>Température</term>
<term>Thiosulfate sulfurtransferase ()</term>
<term>Urée</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term>
<term>Heat-Shock Proteins</term>
<term>Proteins</term>
<term>Thiosulfate Sulfurtransferase</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphate</term>
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<term>Chaperonins</term>
<term>Urea</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adénosine triphosphate</term>
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<term>Protein Conformation</term>
<term>Temperature</term>
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<term>Protéines bactériennes</term>
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<front><div type="abstract" xml:lang="en">In vitro refolding of the urea-unfolded, monomeric, mitochondrial enzyme rhodanese (thiosulfate sulfur-transferase; EC 2.8.1.1) is facilitated by the chaperonin proteins cpn60 and cpn10 from Escherichia coli at 37 degrees C, but the refolding is strongly inhibited at 10 degrees C. In contrast, the unassisted refolding of rhodanese is efficient at 10 degrees C, but the refolding efficiency decreases as the temperature is raised. These observations provided two measures of the cpn60-rhodanese complex. Thus, we monitored either 1) the cpn60-dependent inhibition of spontaneous folding at 10 degrees C or 2) the recovery of active rhodanese in the complete chaperonin system at 25 degrees C, after first forming a cpn60-rhodanese complex at 10 degrees C. These procedures minimized the aggregation of interactive folding intermediates that tend to overestimate the apparent number of cpn60 14-mers in determining the stoichiometry of protein-cpn60 14-mer interactions. Both procedures used here gave results that were consistent with there being 1 rhodanese binding site/cpn60 tetradecamer. This stoichiometry is significantly less than might be expected from the fact that cpn60 is composed of 14 identical subunits, and it may indicate that rhodanese interacts with a restricted region that is formed when the cpn60 tetradecamer is assembled. The ability to stabilize chaperonin-protein complexes that can subsequently be reactivated will aid studies of the mode of action of the ubiquitous chaperonin proteins.</div>
</front>
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<name sortKey="Mendoza, J A" sort="Mendoza, J A" uniqKey="Mendoza J" first="J A" last="Mendoza">J A Mendoza</name>
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Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

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

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