Temperature Regulates Stability, Ligand Binding (Mg²⁺ and ATP), and Stoichiometry of GroEL-GroES Complexes.

ABSTRACT: Chaperonins are nanomachines that harness ATP hydrolysis to power and catalyze protein folding, a chemical action that is directly linked to the maintenance of cell function through protein folding/refolding and assembly. GroEL and the GroEL-GroES complex are archetypal examples of such protein folding machines. Here, variable-temperature electrospray ionization (vT-ESI) native mass spectrometry is used to delineate the effects of solution temperature and ATP concentrations on the stabilities of GroEL and GroEL-GroES complexes. The results show clear evidence for destabilization of both GroEL₁₄ and GroES₇ at temperatures of 50 and 45 °C, respectively, substantially below the previously reported melting temperature (T_m ∼ 70 °C). This destabilization i

SUBMITTER: Walker TE 

PROVIDER: S-EPMC8939001 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature