The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding.

Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli.

AIMS To investigate the factors affecting expression and solubilization of Escherichia coli maltodextrin glucosidase in E. coli. METHODS AND RESULTS Expression level and solubilization of the recombinant E. coli maltodextrin glucosidase was studied in E. coli at different temperatures, in presence of overexpressed GroEL, GroES and externally supplemented glycerol. Aggregation of maltodextrin ...

A Folding & Unfolding Study: Groel-groes Assisted Folding of Multiple Proteins in E. Coli and Irreversible Denaturation of Maltodextrin Glucosidase Megha Goyal Kusuma School of Biological Sciences Indian Institute of Technology Delhi

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.

Although a cis mechanism of GroEL-mediated protein folding, occurring inside a hydrophilic chamber encapsulated by the co-chaperonin GroES, has been well documented, recently the GroEL-GroES-mediated folding of aconitase, a large protein (82 kDa) that could not be encapsulated, was described. This process required GroES binding to the ring opposite the polypeptide (trans) to drive release and p...

Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.

Despite a vast amount information on the interplay of GroEL, GroES, and ATP in chaperone-assisted folding, the molecular details on the conformational dynamics of folding polypeptide during its GroEL/GroES-assisted folding cycle is quite limited. Practically no such studies have been reported to date on large proteins, which often have difficulty folding in vitro. The effect of the GroEL/GroES ...

GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated

The chaperonin GroEL binds nonnative proteins too large to fit inside the productive GroEL-GroES cis cavity, but whether and how it assists their folding has remained unanswered. We have examined yeast mitochondrial aconitase, an 82 kDa monomeric Fe(4)S(4) cluster-containing enzyme, observed to aggregate in chaperonin-deficient mitochondria. We observed that aconitase folding both in vivo and i...