Description
Karolina Drygała, Dorota Bartusik-Aebisher and David AebisherMedical College of The University of Rzeszów, Rzeszów, PolandPart of the book: The Biochemical Guide to ProteinsAbstractGroEL is one of the chaperones that play an essential role in folding non-native proteins and preventing their aggregation. GroEL is a large homotetradecamer composed of two seven-membered rings consisting of two seven-membered 57 kD subunits. It has been found that the first GroES interacting with GroEL does not always dissociate from the symmetric complex prior to dissociation of the second GroES molecule, i.e., dissociation of GroES molecules from this complex may occur in a random order. It was also found that GroEL emerged in three different states: as GroEL itself, as an asymmetric complex and as a symmetric complex. This finding points to the existence of two reaction cycles in the GroEL-GroES interaction: an asymmetric cycle and a symmetric cycle.Keywords: GroEL, monomolecular test, non-native substrate proteins, polypeptidesReferencesFourie K. R., Wilson H. L. Understanding GroEL and DnaK Stress Response Proteins asAntigens for Bacterial Diseases. Vaccines (Basel). 2020 Dec 17;8(4):773.Ishii N. GroEL and the GroEL-GroES Complex. Subcell Biochem. 2017;83:483-504.Nakamoto H., Kojima K. Non-housekeeping, non-essential GroEL (chaperonin) hasacquired novel structure and function beneficial under stress in cyanobacteria. PhysiolPlant. 2017 Nov;161(3):296-310.Thirumalai D., Lorimer G. H., Hyeon C. Iterative annealing mechanism explains thefunctions of the GroEL and RNA chaperones. Protein Sci. 2020 Feb;29(2):360-377.Yan X., Shi Q., Bracher A., Miličić G., Singh A. K., Hartl F. U., Hayer-Hartl M. GroELRing Separation and Exchange in the Chaperonin Reaction. Cell. 2018 Jan25;172(3):605-617.e11.
