Molecular chaperones and especially chaperonins are primarily known as
special members of the family of heat shock proteins which participate in folding,
assembly, transmembrane transport and degradation of a wide variety of cellular
proteins both in prokaryotes and eukaryotes. The multifunctional character of
chaperones underlies their involvement in many diseases. One of their functions is
binding to polypeptides lacking a rigid tertiary structure, i.e., to those with many
exposed hydrophobic amino acids. The current review is focused on interaction of
polypeptides of this type with GroEL, the best-studied Escherichia coli chaperonin.
The literature data on driving forces of their interaction, localization of substrate
polypeptides on the GroEL surface, and the effect of GroEL ligands on its interaction
with substrate polypeptides are considered. Some biotechnological applications of this
event are also discussed.
Keywords: Protein folding, Chaperones, GroEL chaperonin, Protein-protein
interaction.
