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

FEBS Letters

Hemmingsen, Sean M.¹  Lissin, Nikolai M.² 

[1] Plant Biotechnology Institute, National Research Council Canada, 110 Gymnasium Place, Saskatoon, Saskatchewan, S7N OW9, Canada;Institute of Protein Research, Academy of Sciences of Russia, 142292 Pushchino, Moscow Region, Russian Federation

关键词: Molecular chaperone;    Chaperonin;    GroEL;    Self-assembly;    Protein folding;    ATP;    EDTA;    ethylenediaminetetraacetic acid;    DTT;    dithiothreitol;    SDS;    sodium dodecyl sulfate;    β-ME;    β-mercaptoethanol;    ATP-γ-S;    adenosine 5'-O-(3-thiotriphosphate);   

DOI  :  10.1016/0014-5793(93)81528-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown