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....

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1992-11, Vol.89 (21), p.10341-10344
Hauptverfasser:	Gragerov, Alexander, Nudler, Evgeny, Komissarova, Natalia, Gaitanaris, George A., Gottesman, Max E., Nikiforov, Vadim
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Analytical, structural and metabolic biochemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences Cell aggregates Chaperonin 10 Chaperonin 60 DnaJ protein DnaK protein Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Gene Deletion Genes, Bacterial Genetics Genotype GroEL protein GroES protein Heat shock proteins Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins Medical research Miscellaneous Operons Overproduction Plasmids Protein Folding Proteins Solubility
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Beschreibung
Zusammenfassung:	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.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.89.21.10341