Chaperonin Escherichia coli

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. 

Only recently have heat shock proteins been used in the stabilization of nanoparticles. Aida et al. have demonstrated the inclusion of already preformed CdS nanoparticles within the chaperonin proteins of GroEL from Escherichia coli and T.th cpn from Thermus thermophilus HB8. These proteins were chosen as a result of sharing similar structural characteristics (1) tubular structure measuring 14.6nm in length, (2) cylindrical cavity with a 4.5-nm diameter, and (3) stability to adverse conditions (pH and temperature). T.th cpn, however, contains an additional bowl-shaped capping protein. 

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