Title: The Lower Hydrolysis of ATP by the Stress Protein GroEL Is a Major Factor Responsible for the Diminished Chaperonin Activity at Low Temperature
Abstract: The chaperonins GroEL and GroES were shown to facilitate the refolding of urea-unfolded rhodanese in an ATP-dependent process at 25 or 37°C. A diminished chaperonin activity was observed at 10°C, however. At low temperature, GroEL retains its ability to form a complex with urea-unfolded rhodanese or with GroES. GroEL is also able to bind ATP at 10°C. Interestingly, the ATPase activity of GroEL was highly decreased at low temperatures. Hydrolysis of ATP by GroEL was 60% less at 10°C than at 25°C. We conclude that the reduced hydrolysis of ATP by GroEL is a major but perhaps not the only factor responsible for the diminished chaperonin activity at 10°C. GroEL may function primarily at higher temperatures in which the ability of GroEL to hydrolyze ATP is not compromised.
Publication Year: 2000
Publication Date: 2000-12-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 24
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