@article{89721,
  keywords = {Escherichia coli, Anti-Bacterial Agents, Membrane Proteins, Mutant Proteins, Recombinant Fusion Proteins, Escherichia coli Proteins, beta-Galactosidase, Heat-Shock Proteins, Protein Transport, Protein Sorting Signals, Bacterial Outer Membrane Proteins, Receptors, Virus, Serine Endopeptidases, SEC Translocation Channels, ATP-Dependent Proteases, Chloramphenicol, Periplasmic Proteins, Porins, Tetracycline},
  author = {van Johna Stelten and Filo Silva and Dominique Belin and Thomas Silhavy},
  title = {Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY},
  abstract = {<p>Protein secretion occurs via translocation by the evolutionarily conserved Sec complex. LacZ hybrid proteins have long been used to study translocation in Escherichia coli. Some LacZ hybrids were thought to block secretion by physically jamming the Sec complex, leading to cell death. We found that jammed Sec complexes caused the degradation of essential translocator components by the protease FtsH. Increasing the amounts or the stability of the membrane protein YccA, a known inhibitor of FtsH, counteracted this destruction. Antibiotics that inhibit translation elongation also jammed the translocator and caused the degradation of translocator components, which may contribute to their effectiveness. Intriguingly, YccA is a functional homolog of the proto-oncogene product Bax Inhibitor-1, which may share a similar mechanism of action in regulating apoptosis upon prolonged secretion stress.</p>
},
  year = {2009},
  journal = {Science},
  volume = {325},
  pages = {753-6},
  month = {08/2009},
  issn = {1095-9203},
  doi = {10.1126/science.1172221},
  language = {eng},
}