PMID:8099330
| Citation |
Lissin, NM and Hemmingsen, SM (1993) Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides. FEBS Lett. 324:41-4 |
|---|---|
| Abstract |
E. coli GroEL chaperonin monomers, isolated after urea-induced dissociation of GroEL14, undergo cold denaturation below 5 degrees C. Above 5 degrees C, these monomers undergo MgATP-dependent self-assembly. We have demonstrated a conformational transition at 0 degree 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 degrees 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 degrees C is required for GroEL to undergo oligomerization. |
| Links | |
| Keywords |
Adenine Nucleotides/pharmacology; Adenosine Diphosphate/pharmacology; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/pharmacology; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Chaperonin 60; Cold Temperature; Escherichia coli/genetics; Escherichia coli/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/isolation & purification; Heat-Shock Proteins/metabolism; Magnesium/pharmacology; Protein Conformation; Protein Denaturation |
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