Article
Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.
Proceedings of the National Academy of Sciences of the United States of America - 1 Nov 1992
Gragerov A, Nudler E, Komissarova N, Gaitanaris G A, Gottesman M E, Nikiforov V
Abstract excerpt
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...
Topics
- Bacterial Proteins
- Chaperonin 10
- Chaperonin 60
- Escherichia coli
- Escherichia coli Proteins
- Gene Deletion
- Genes, Bacterial
- Genotype
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins