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Chaperonin and cochaperonin, represented by  E .  coli  GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroEL SR  forms a stable complex with GroES, arresting the chaperoning reaction cycle. GroES I25 interacts with GroEL; however, mutations of I25 abolish GroES-GroEL interaction due to the seven-fold mutational amplification in heptameric GroES. To weaken GroEL SR -GroES interaction in a controlled manner, we used  groES   7 , a gene linking seven copies of  groES , to incorporate I25 mutations in selected GroES modules in GroES 7 . We generated GroES 7  variants with different numbers of GroESI25A or GroESI25D modules and different arrangements of the mutated modules, and biochemically characterized their interactions with GroEL SR . GroES 7  variants with two mutated modules participated in GroEL SR –mediated protein folding  in vitro . GroES 7  variants with two or three mutated modules collaborated with GroEL SR  to perform chaperone function  in vivo : three GroES 7  variants functioned with GroEL SR  under both normal and heat-shock conditions. Our studies on functional single-ring bacterial chaperonin systems are informative to the single-ring human mitochondrial chaperonin mtHsp60-mtHsp10, and will provide insights into how the double-ring bacterial system has evolved to the single-ring mtHsp60-mtHsp10.

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction