Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.
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.
Institute of Molecular Genetics, Russian Academy of Sciences, Moscow.
A
A
Gragerov
E
E
Nudler
N
N
Komissarova
G A
GA
Gaitanaris
M E
ME
Gottesman
V
V
Nikiforov
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D018835:Chaperonin 10; D018834:Chaperonin 60; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D017353:Gene Deletion; D005798:Genes, Bacterial; D005838:Genotype; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; C494635:DnaJ protein, E coli; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C063842:dnaK protein, E coli