GroEl proteins

Bochkareva, E,S., Lisson, N.M., Girshovich, A.S. (1988). Transient association of newly synthesized unfolded proteins with the heat shock GroEL protein. Nature 336, 254—257. 

How does the GroEL-GroES complex function as a chaperone to assist protein folding Although several aspects of the mechanism are not clear, the main features of the functional cycle are known. The first step is the... 

Chen, S. et al. Eocation of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371 261-264, 1994. 

Enzymes assist formation of proper disulfide bonds during folding Isomerization of proline residues can be a rate-limiting step in protein folding Proteins can fold or unfold inside chaperonins GroEL is a cylindrical structure with a... 

Hallett, P., Mehlert, A., Maxwell, A. (1990). E. colt cells resistant to the DNA gyrase inhibitor, ciprofloxacin, overproduce a 60 IcD protein homologous to GroEL. Mol. Microbiol. 4,345-353. 

Langer, T., Lu., C, Echols, H., Flanagan, J, Hayer, M.K., Hartl, F.-U. (1992). Successive action of Dnak, DnaJ, GroEL along the pathway of chaperone mediated protein folding. Nature 356, 683-689. 

Yu, M., Goldberg, S., Goldberg, A.L. (1W2). Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation. Nature 357, 167-169. 

NifH and NifDK to GroEL. It is not clear from these data at which stage in the biosynthetic pathway just described GroEL might be involved in MoFe protein maturation, but it could be during P cluster insertion. 

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