@article{199206,
  keywords = {Kinetics, Genes, Mutation, Escherichia coli, Genes, Bacterial, Transcription, Genetic, Species Specificity, Phenotype, beta-Galactosidase, Genotype, Genes, Lethal, Bacteriophage lambda, Galactosidases},
  author = {Kiino and Silhavy},
  title = {Mutation prlF1 relieves the lethality associated with export of beta-galactosidase hybrid proteins in Escherichia coli},
  abstract = {<p>The 42-1 lamB-lacZ gene fusion confers a conditionally lethal, export-dependent phenotype known as maltose sensitivity. A maltose-resistant mutant showing decreased beta-galactosidase activity of the hybrid protein, designated prlF1 (protein localization), was unlinked to the lamB-lacZ fusion. This mutation mapped at 70 min on the Escherichia coli linkage map and conferred maltose resistance, a 30-fold reduction in beta-galactosidase activity, and a 30\% decrease in cellular growth rate at 30 degrees C that was independent of the presence of a gene fusion. prlF1 also decreased the beta-galactosidase activity and relieved the maltose sensitivity conferred by fusions of lacZ to the gene specifying the periplasmic maltose-binding protein, malE. The decrease in beta-galactosidase activity, however, was specific for exported hybrid proteins. When export of the hybrid protein was blocked by a signal sequence mutation, prlF1 decreased the beta-galactosidase activity only 2.5-fold. Similarly, prlF1 did not affect the beta-galactosidase activity of fusions of lacZ to a gene specifying a nonexported protein, malK.</p>
},
  year = {1984},
  journal = {J Bacteriol},
  volume = {158},
  pages = {878-83},
  month = {06/1984},
  issn = {0021-9193},
  doi = {10.1128/jb.158.3.878-883.1984},
  language = {eng},
}