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Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY

van Stelten, Johna
Silva, Filo
Silhavy, T. J.
Published in Science. 2009, vol. 325, no. 5941, p. 753-756
Abstract 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.
Keywords ATP-Dependent Proteases/metabolismAnti-Bacterial Agents/ pharmacologyBacterial Outer Membrane Proteins/genetics/metabolismChloramphenicol/pharmacologyEscherichia coli/ drug effects/genetics/ metabolismEscherichia coli Proteins/genetics/ metabolismHeat-Shock Proteins/genetics/metabolismMembrane Proteins/genetics/ metabolismMutant Proteins/metabolismPeriplasmic Proteins/genetics/metabolismPorins/genetics/metabolismProtein Sorting SignalsProtein Transport/drug effectsReceptors, Virus/genetics/metabolismRecombinant Fusion Proteins/metabolismSerine Endopeptidases/genetics/metabolismTetracycline/pharmacologybeta-Galactosidase/genetics/metabolism
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Other version: http://www.sciencemag.org/cgi/reprint/325/5941/753.pdf
PMID: 19661432
Research group Translocation des protéines à travers les membranes (169)
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