@article{89986,
  keywords = {Base Sequence, Bacterial Proteins, signal transduction, Mutation, Escherichia coli, Molecular Sequence Data, Protein Kinases, Gene Expression Regulation, Bacterial, Amino Acid Sequence, Escherichia coli Proteins, Enzyme Activation, beta-Galactosidase, Consensus Sequence, Open Reading Frames, Heat-Shock Proteins, Lipoproteins, Plasmids, Maltose, Bacterial Outer Membrane Proteins, Transcriptional Activation, Suppression, Genetic, Serine Endopeptidases, Periplasmic Proteins, Enzyme Repression},
  author = {Snyder and Davis and Danese and Cosma and Silhavy},
  title = {Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway},
  abstract = {<p>The LamB-LacZ-PhoA tripartite fusion protein is secreted to the periplasm, where it exerts a toxicity of unknown origin during high-level synthesis in the presence of the inducer maltose, a phenotype referred to as maltose sensitivity. We selected multicopy suppressors of this toxicity that allow growth of the tripartite fusion strains in the presence of maltose. Mapping and subclone analysis of the suppressor locus identified a previously uncharacterized chromosomal region at 4.7 min that is responsible for suppression. DNA sequence analysis revealed a new gene with the potential to code for a protein of 236 amino acids with a predicted molecular mass of 25,829 Da. The gene product contains an amino-terminal signal sequence to direct the protein for secretion and a consensus lipoprotein modification sequence. As predicted from the sequence, the suppressor protein is labeled with [3H]palmitate and is localized to the outer membrane. Accordingly, the gene has been named nlpE (for new lipoprotein E). Increased expression of NlpE suppresses the maltose sensitivity of tripartite fusion strains and also the extracytoplasmic toxicities conferred by a mutant outer membrane protein, LamBA23D. Suppression occurs by activation of the Cpx two-component signal transduction pathway. This pathway controls the expression of the periplasmic protease DegP and other factors that can combat certain types of extracytoplasmic stress.</p>
},
  year = {1995},
  journal = {J Bacteriol},
  volume = {177},
  pages = {4216-23},
  month = {08/1995},
  issn = {0021-9193},
  doi = {10.1128/jb.177.15.4216-4223.1995},
  language = {eng},
}