@article{90086,
  keywords = {Biological Transport, Escherichia coli, Recombinant Fusion Proteins, Escherichia coli Proteins, Carrier Proteins, ATP-Binding Cassette Transporters, beta-Galactosidase, Heat-Shock Proteins, Plasmids, Maltose, Maltose-Binding Proteins, Protein Sorting Signals, Monosaccharide Transport Proteins, Transformation, Bacterial},
  author = {Phillips and Silhavy},
  title = {Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli},
  abstract = {<p>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.</p>
},
  year = {1990},
  journal = {Nature},
  volume = {344},
  pages = {882-4},
  month = {04/1990},
  issn = {0028-0836},
  doi = {10.1038/344882a0},
  language = {eng},
}