Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides

DOI	Trouver le DOI : https://doi.org/10.1016/0014-5793(93)81528-8
Auteur	Rechercher : Lissin, Nikolai M.¹; Rechercher : Hemmingsen, Sean M.¹
Affiliation	Conseil national de recherches du Canada. Institut de biotechnologie des plantes du CNRC
Format	Texte, Article
Sujet	molecular chaperone; chaperonin; GroEL; self-assembly; protein folding; ATP
Résumé	E. coli GroEL chaperonin monomers, isolated after urea-induced dissociation of GroEL₁₄, undergo cold denaturation below 5° C. Above 5°C, these monomers undergo MgATP-dependent self-assembly. We have demonstrated a conformational transition at 0°C induced by interaction of monomeric GroEL with adenine nucleotides. This conformation has a dramatically decreased Stokes radius and enhanced resistance to trypsin but it is slightly less compact than the conformation of monomers at 23°C in the absence of MgATP and it is not capable of spontaneous self-assembly. A second, temperature-dependent conformational change with a transition at about 5°C is required for GroEL to undergo oligomerization.
Date de publication	1993-06-07
Maison d’édition	Wiley
Dans	FEBS Letters 324, nº 1 (7 juin 1993) : 41–44.
Langue	anglais
Publications évaluées par des pairs	Oui
Identificateur	NRCC-35896
Exporter la notice	Exporter en format RIS
Signaler une correction	Signaler une correction (s'ouvre dans un nouvel onglet)
Identificateur de l’enregistrement	6be0d029-1072-4089-b2c6-25587d11140e
Enregistrement créé	2023-11-06
Enregistrement modifié	2023-11-06