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Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

1992; National Academy of Sciences; Volume: 89; Issue: 21 Linguagem: Inglês

10.1073/pnas.89.21.10341

1091-6490

A. I. Gragerov, Evgeny Nudler, N. V. Komissarova, George Gaitanaris, Max E. Gottesman, Vadim Nikiforov,

thermodynamics and calorimetric analyses

Newly synthesized proteins aggregate extensively in Escherichia coli rpoH mutants, which are deficient in the heat shock proteins (hsp). Overproduction of either GroEL and GroES or DnaK and DnaJ prevents aggregation. If expressed together, the four hsp are effective at physiological concentrations. Our data suggest that the GroEL and GroES proteins and the DnaK and DnaJ proteins have complementary functions in the folding and assembly of most proteins.