In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.
Identifieur interne : 000323 ( France/Analysis ); précédent : 000322; suivant : 000324In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.
Auteurs : N M Lissin [France]Source :
- FEBS letters [ 0014-5793 ] ; 1995.
Descripteurs français
- KwdFr :
- ADP (métabolisme), Adénosine triphosphate (métabolisme), Basse température, Chaperonine-60 (), Chaperonine-60 (métabolisme), Chloroplastes (métabolisme), Conformation des protéines, Escherichia coli (), Magnésium (métabolisme), Mitochondries (métabolisme), Pois, Saccharomyces cerevisiae, Urée (pharmacologie).
- MESH :
- métabolisme : ADP, Adénosine triphosphate, Chaperonine-60, Chloroplastes, Magnésium, Mitochondries.
- pharmacologie : Urée.
- Basse température, Chaperonine-60, Conformation des protéines, Escherichia coli, Pois, Saccharomyces cerevisiae.
English descriptors
- KwdEn :
- Adenosine Diphosphate (metabolism), Adenosine Triphosphate (metabolism), Chaperonin 60 (chemistry), Chaperonin 60 (metabolism), Chloroplasts (metabolism), Cold Temperature, Escherichia coli (chemistry), Magnesium (metabolism), Mitochondria (metabolism), Peas, Protein Conformation, Saccharomyces cerevisiae, Urea (pharmacology).
- MESH :
- chemical , chemistry : Chaperonin 60.
- chemical , metabolism : Adenosine Diphosphate, Adenosine Triphosphate, Chaperonin 60, Magnesium.
- chemistry : Escherichia coli.
- metabolism : Chloroplasts, Mitochondria.
- chemical , pharmacology : Urea.
- Cold Temperature, Peas, Protein Conformation, Saccharomyces cerevisiae.
Abstract
A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.
DOI: 10.1016/0014-5793(95)00151-x
PubMed: 7890040
Affiliations:
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pubmed:7890040Le document en format XML
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when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate (metabolism)</term><term>Adenosine Triphosphate (metabolism)</term><term>Chaperonin 60 (chemistry)</term><term>Chaperonin 60 (metabolism)</term><term>Chloroplasts (metabolism)</term><term>Cold Temperature</term><term>Escherichia coli (chemistry)</term><term>Magnesium (metabolism)</term><term>Mitochondria (metabolism)</term><term>Peas</term><term>Protein Conformation</term><term>Saccharomyces cerevisiae</term><term>Urea (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADP (métabolisme)</term><term>Adénosine triphosphate (métabolisme)</term><term>Basse température</term><term>Chaperonine-60 ()</term><term>Chaperonine-60 (métabolisme)</term><term>Chloroplastes (métabolisme)</term><term>Conformation des protéines</term><term>Escherichia coli ()</term><term>Magnésium (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Pois</term><term>Saccharomyces cerevisiae</term><term>Urée (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chaperonin 60</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate</term><term>Adenosine Triphosphate</term><term>Chaperonin 60</term><term>Magnesium</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADP</term><term>Adénosine triphosphate</term><term>Chaperonine-60</term><term>Chloroplastes</term><term>Magnésium</term><term>Mitochondries</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Urée</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Urea</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cold Temperature</term><term>Peas</term><term>Protein Conformation</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Basse température</term><term>Chaperonine-60</term><term>Conformation des protéines</term><term>Escherichia coli</term><term>Pois</term><term>Saccharomyces cerevisiae</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Lissin, N M" sort="Lissin, N M" uniqKey="Lissin N" first="N M" last="Lissin">N M Lissin</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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