The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures

Biochemical and Biophysical Research Communications
J A MendozaP Dulin

Abstract

The chaperonin GroEL is a heat-shock protein that stabilizes folding intermediates by forming binary complexes. The release of bound polypeptides as active proteins requires ATP hydrolysis by GroEL. The ability of GroEL to support the folding of urea-unfolded rhodanese and to hydrolyze ATP was investigated at high temperatures. We found that the chaperonin-mediated folding of rhodanese and the ATPase activity of GroEL are temperature dependent. The GroEL ATPase activity, however, increases very strongly over the range of temperatures that is physiologically relevant for Escherichia coli growth. Further, GroES partially suppresses the GroEL ATPase activity in the same temperature range.

Citations

Apr 19, 2005·The International Journal of Biochemistry & Cell Biology·Girish C MelkaniJose A Mendoza
Mar 30, 2006·Journal of Bioscience and Bioengineering·Jiro KohdaTakuo Yano
Jan 26, 2012·Bioscience Reports·Girish C MelkaniJose A Mendoza
Feb 23, 2002·Protein Expression and Purification·Celeste WeissAbdussalam Azem
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Oct 12, 2014·Archives of Microbiology·Lei TanChan Ding
Jan 23, 1999·European Journal of Biochemistry·A GalánA Muga
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Apr 28, 1997·FEBS Letters·P GoloubinoffA Azem
Jul 11, 2006·Biochemical and Biophysical Research Communications·Girish C MelkaniJose A Mendoza

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