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

A Gragerov; E Nudler; N Komissarova; G A Gaitanaris; M E Gottesman; V Nikiforov

doi:10.1073/pnas.89.21.10341

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

Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10341-4. doi: 10.1073/pnas.89.21.10341.

Authors

A Gragerov¹, E Nudler, N Komissarova, G A Gaitanaris, M E Gottesman, V Nikiforov

Affiliation

¹ Institute of Molecular Genetics, Russian Academy of Sciences, Moscow.

Abstract

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.

MeSH terms

Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Chaperonin 10
Chaperonin 60
Escherichia coli / genetics
Escherichia coli / metabolism*
Escherichia coli Proteins*
Gene Deletion
Genes, Bacterial
Genotype
HSP40 Heat-Shock Proteins
HSP70 Heat-Shock Proteins*
Heat-Shock Proteins / genetics
Heat-Shock Proteins / metabolism*
Protein Folding*

Substances

Bacterial Proteins
Chaperonin 10
Chaperonin 60
DnaJ protein, E coli
Escherichia coli Proteins
HSP40 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
dnaK protein, E coli