Release of both native and non-native proteins from a cis-only GroEL ternary complex

Article Abstract:

The ternary GroEL-GroES-polypeptide complex converts a part of the substrate polypeptide into the native state during each chaperonin cycle, and releases the remaining part as non-native forms in Xenopus oocyte extracts. The non-native forms help in kinetic partitioning of the polypeptide among various chaperones and proteolytic components. The partitioning also influences the conformation and lifetime of a protein. The cis-only mixed-ring GroEL complex binds the polypeptide and GroES on one of its two rings and mediates refolding of rhodanese.

Observations, Proteins, Xenopus, Polypeptides

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The crystal structure of the asymmetric GroEL-GroES-(APD)7 chaperonin complex

Article Abstract:

Chaperonins exists as multi-subunit protein assemblies, assisting in protein folding with the consumption of ATP. Asymmetric intermediates of GroEL are formed with GroES, the co-chaperonin, and nucleotides bound to one of seven-subunit rings in Escherichia coli, but not to the trans ring, or opposing ring. The GroEl-GroES-(ADP) 7 structures shows that en bloc cis ring movements help bound GroES to stabilize a folding chamber, showing important bacterial chaperonin-assisted protein folding cycle features.

Methods, Physiological aspects, Eukaryotic cells, Cells (Biology), Eukaryotes

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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

Article Abstract:

The central cavity in each ring of the chaperonin GroEL provides an environment for efficient protein folding when capped by co-chaperone GroES, particularly when adenine nucleotides are present.Rhodanese folding has been observed in cis ternary complexes where GroES and polypeptide are linked to the same ring, formed with ATP, ADP or non-hydrolysable ATP analogues. Malate dehydrogenase and Rubisco folding requires ATP in the cis ring to form a GroEL-ADP-GroES complex with decreased stability.

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