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

Johna Van Stelten, Filo Silva, Dominique Belin, Thomas J. Silhavy

Research output: Contribution to journalArticle

74 Scopus citations

Abstract

Protein secretion occurs via translocation by the evolutionary 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.

Original languageEnglish (US)
Pages (from-to)753-756
Number of pages4
JournalScience
Volume325
Issue number5941
DOIs
StatePublished - 2009

All Science Journal Classification (ASJC) codes

  • General

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