GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. [5] It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES.

GroEL may be engineered for stabilization, biosynthesis, or soluble expression of polypeptides in any of its forms: as a full-sized oligomer, a monomer, or a separate apical domain, called a minichaperone. All these cases are described in detail below.

Aug 28, 2009 · We demonstrate here that the inability of M. tuberculosis GroEL1 to act as a functional chaperone in E. coli can be alleviated by facilitated oligomerization.

Apr 22, 2014 · Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself. According to the literature, GroEL reassembly is dependent on chaperonin ligands and solvent composition.

GroEL is an all‐purpose stochastic machine that assists misfolded substrate proteins to fold. The RNA chaperones such as CYT‐19, which are ATP‐consuming enzymes, help the folding of ribozymes that get trapped in metastable states for long times.

Nov 1, 2024 · GroEL regulates gene expression at the post-transcriptional level and its activity is conserved in Shigella. Chaperonins are evolutionarily conserved proteins that facilitate polypeptide assemblies. The most extensively studied chaperonin is GroEL, which plays a crucial role in Escherichia coli.

Oct 28, 2023 · Therefore, we describe an approach to assess bacterial community compositions at the family level using the taxonomic marker protein GroEL, which is ubiquitously found in bacteria, except a few obligate intracellular species. We …

GroEL has become the most examined and standard chaperonin in the field of chaperone-mediated protein folding. This chapter describes a purification protocol by which it is possible to obtain pure GroEL from an overproducing strain of E. coli.

The chaperonin system GroEL-GroES is present in all kingdoms of life and rescues proteins from improper folding and aggregation upon internal and external stress conditions, including high ...

Nov 30, 2021 · Here I describe an easy-to-carry-out purification protocol that can reliably produce highly purified and fully functional GroEL protein in large quantities.