Polypeptides, GroEL binding

GroEL is a cylindrical structure with a central channel in which newly synthesized polypeptides bind... 

Fenton, W.A., et al. Residues in chaperonin GroEL required for polypeptide binding and release. 

W. A. Fenton, Y. Kashi, K. Furtak, and A. L. Horwich, Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619 (1994). 

The GroEL-GroES complex binds and releases newly synthesized polypeptides in an ATP-dependent cycle... 

Several conclusions can be reached from this study. First, multiple GroEL apical domains indeed bind to substrate polypeptides, both in vivo and in vitro, and this ability appears to be crucial to the cellular function of GroEL. This is supported by the additional demonstration that non-native Rubisco bound to a GroEL containing an apical cysteine residue made disulfide crosslinks to multiple GroEL subunits. Second, different substrates have different requirements for the apical domains, stringent substrates such as MDH and Rubisco being the most... 

Another intriguing facet of polypeptide-GroEL interaction is the effect of binding on the structure of the non-native substrate. It is conceivable that the chaperonin, like other cellular chaperones, is a passive... 

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