Chaperonins: Nanocarriers with Biotechnological Applications

Abstract

Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins. Chaperonins are found in two main conformations, one in which the cavity is open and ready to recognise and trap unfolded client proteins, and a “closed” form in which folding takes place. The conspicuous properties of this structure (a cylinder containing a cavity that allows confinement) and the potential to control its closure and aperture have inspired a number of nanotechnological applications that will be described in this review.

Molecular Bases of Heat Stress Responses in Vegetable Crops With Focusing on Heat Shock Factors and Heat Shock Proteins

“…Chaperonins are generally composed of two rings, stacked back to back, consisting of subunits of ∼60 kDa molecular weight ( Nguyen et al, 2021 ). Each oligomer has three domains (1) the equatorial domain (ED), which has the ATP-biding site, (2) the apical domain (AD), which hosts client proteins and (3) the intermediate domain (ID), which transduces signals from the equatorial domain ( Pipaón et al, 2021 ). When signals are transmitted to the ID from ATP binding and hydrolysis, conformational changes occur in the AD corresponding to the open and closed forms ( Xu et al, 1997 ).…”

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

“…Group I chaperonins constitute a large family of highly conserved ~60-kDa essential proteins that typically reside in the bacterial cytoplasm, or the organellar matrix. They team-up with the equally conserved ~10-kDa essential co-chaperonins, to self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins, and have recently found some biotechnological applications, as reviewed by Horwich and Fenton, and Pipaón et al [ 1 , 2 ]. Each nanobox comprises a barrel of 14 chaperonin subunits (in turn formed by two heptameric rings), and two lids (each formed by seven co-chaperonin subunits) that close the barrel ends.…”

“…Each nanobox comprises a barrel of 14 chaperonin subunits (in turn formed by two heptameric rings), and two lids (each formed by seven co-chaperonin subunits) that close the barrel ends. Inside the closed barrel, favorable conditions are provided for the folding of nascent polypeptides, or the re-folding of denatured proteins, in an ATP-mediated process [ 1 , 2 , 3 , 4 ]. The GroEL/GroES protein folding machinery of the bacterium Escherichia coli is the best characterized group I chaperonin/co-chaperonin complex.…”