Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.
basic_science · Level V
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- Record sourced from PubMed, PMID 1359538.
- Also identified by PMC identifier 50334.
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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.
Medical subject headings
- Bacterial Proteins
- Escherichia coli
- Escherichia coli Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Protein Folding