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J. Biol. Chem., Vol. 276, Issue 7, 4981-4987, February 16, 2001

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The Importance of a Mobile Loop in Regulating Chaperonin/ Co-chaperonin Interaction
HUMANS VERSUS ESCHERICHIA COLI^*

Alexandra Richardson, Françoise Schwager, Samuel J. Landry, and Costa Georgopoulos^§

From the Département de Biochimie Médicale, Centre Médical Universitaire, 1 rue Michel-Servet, 1211 Geneva, Switzerland and the  Department of Biochemistry, Tulane University School of Medicine, New Orleans, Louisiana 70112

Chaperonins are universally conserved proteins that nonspecifically facilitate the folding of a wide spectrum of proteins. While bacterial GroEL is functionally promiscuous with various co-chaperonin partners, its human homologue, Hsp60 functions specifically with its co-chaperonin partner, Hsp10, and not with other co-chaperonins, such as the bacterial GroES or bacteriophage T4-encoded Gp31. Co-chaperonin interaction with chaperonin is mediated by the co-chaperonin mobile loop that folds into a -hairpin conformation upon binding to the chaperonin. A delicate balance of flexibility and conformational preferences of the mobile loop determines co-chaperonin affinity for chaperonin. Here, we show that the ability of Hsp10, but not GroES, to interact specifically with Hsp60 lies within the mobile loop sequence. Using mutational analysis, we show that three substitutions in the GroES mobile loop are necessary and sufficient to acquire Hsp10-like specificity. Two of these substitutions are predicted to preorganize the -hairpin turn and one to increase the hydrophobicity of the GroEL-binding site. Together, they result in a GroES that binds chaperonins with higher affinity. It seems likely that the single ring mitochondrial Hsp60 exhibits intrinsically lower affinity for the co-chaperonin that can be compensated for by a higher affinity mobile loop.

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