PMID:2109835
| Citation |
Phillips, GJ and Silhavy, TJ (1990) Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. Nature 344:882-4 |
|---|---|
| Abstract |
The use of lacZ gene fusions, producing a hybrid protein containing an amino terminus specified by a target gene fused to the functional carboxy terminus of beta-galactosidase, has facilitated the study of protein targeting in various organisms. One of the best characterized fusions in Escherichia coli is phi(lamB-lacZ)42-1(Hyb), which produces a hybrid protein with the signal sequence and 181 N-terminal amino acids of the exported protein LamB, attached to LacZ. In common with other LacZ hybrids, the LamB-LacZ(42-1) protein is poorly exported from E. coli, conferring a Lac+ phenotype. beta-Galactosidase activity decreases markedly when cells producing the LamB-LacZ protein are grown at 42 degrees C or when a heat-shock response is induced at lower temperatures by overproducing heat-shock factor RpoH3, indicating the LacZ hybrids are being efficiently targeted to the cell envelope. We now report that the heat-shock proteins DnaK and GroEL can, in sufficient amounts, decrease beta-galactosidase activity and facilitate the export of lacZ-hybrid proteins. |
| Links |
PubMed Online version:10.1038/344882a0 |
| Keywords |
ATP-Binding Cassette Transporters; Biological Transport/physiology; Carrier Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/physiology; Maltose/pharmacology; Maltose-Binding Proteins; Monosaccharide Transport Proteins; Plasmids; Protein Sorting Signals/metabolism; Recombinant Fusion Proteins/metabolism; Transformation, Bacterial; beta-Galactosidase/metabolism |
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