Recombinant Escherichia coli 60 kDa chaperonin (groL)

1. study confirmed the altered GroEL dependence of green fluorescent protein variants with in vitro folding assays; mutations at positions predicted to be highly frustrated were found to correlate with decreased GroEL dependence; conversely, mutations at positions with low frustration were found to correlate with increased GroEL dependence PMID: 29066625
2. In the case of GroEL, individualisation of monomers thus leads to individualisation of homomultimeric protein complexes, effectively providing the prerequisites for evolving an orthogonal intracellular GroEL folding machine. PMID: 24151180
3. Investigated the role of the surface-associated GroEL in the binding of E. coli to macrophages. Results showed that GroEL on E. coli was recognized by LOX-1 on macrophages, leading to the phagocytosis of pathogen by macrophages. PMID: 23085345
4. Nuclear magnetic resonance (NMR) observation of the uniformly (2) H,(15) N-labeled stringent 33-kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1. PMID: 21633984
5. Localization of GroEL protein at possible cell division sites in penicillin treated E. coli cells suggest a possible role of the GroEL protein in cell division. PMID: 15330853
6. the strong binding of N-terminal head protein sequences to GroEL has a role in promoting protein folding PMID: 15571729
7. C-terminal segment of the GroEL equatorial domain has an important role in the temperature dependence of GroEL; E. coli acquired the ability to grow at low temperature through the introduction of cold-adapted chimeric or L524I mutant groEL genes. PMID: 15618620
8. GroEL bound hDHFR might best be described as a dynamic ensemble of randomly structured conformers PMID: 16116078
9. The natural substrate proteins for the Escherichia coli chaperonin GroEL were predicted. PMID: 16537402
10. The data suggest that LDH can be successfully reactivated due to the binding of the denatured molecules to the apical domain of the opposite GroEL ring with their subsequent release into the solution without encapsulation (trans-mechanism). PMID: 16551514
11. These results indicate that GroEL has at least two distinct open-conformations in the presence of nucleotide; ATP-bound prehydrolysis open-form and ADP-bound open-form, and the ATP hydrolysis in open-form destabilizes its open-conformation. PMID: 16977315
12. GroEL function supports the proper folding of a majority of newly translated polypeptides PMID: 17043235
13. yield of the native state in the expanded GroEL cavity is relatively small even after it remains in it for twice the spontaneous folding time PMID: 17496143
14. biophysical analysis of how allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations PMID: 17557788
15. the hydrophilic nature of 526 KNDAAD 531 residues in the flexible C-terminal region is important for proper protein folding within the central cavity of GroEL PMID: 18184659
16. Forced protein unfolding is thus a central component of the multilayered stimulatory mechanism used by GroEL to drive protein folding. PMID: 18311152
17. Results describe the concerted release of substrate domains from GroEL by ATP. PMID: 18556021
18. GroEL provides a platform for obtaining initial glimpses of a membrane protein structure in the absence of lipids or detergents and can function as a scaffold for higher-resolution structural analysis of the protective antigen pore. PMID: 18568038

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KEGG: ecj:JW4103

STRING: 316385.ECDH10B_4336