Article
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.
Cell - 29 Jul 2005
Kerner Michael J, Naylor Dean J, Ishihama Yasushi, Maier Tobias, Chang Hung-Chun, Stines Anna P, Georgopoulos Costa, Frishman Dmitrij, Hayer-Hartl Manajit, Mann Matthias, Hartl F Ulrich
Abstract excerpt
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like structure. Here we define the contribution of this system to protein folding across the entire E. coli proteome. Approximately 250 different proteins interact with GroEL, but most of these can utilize either GroEL or the upstream chaperones trigger factor (TF) and DnaK for folding....
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