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

Full 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.

Author information

Author/s: van Stelten, Johna (J); Silva, Filo (F); Belin, Dominique (D); Silhavy, Thomas J (TJ);

Affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.

Journal: Science (New York, N.Y.) (Science), published in United States. (Language: eng)

Reference: 2009-Aug; vol 325 (issue 5941) : pp 753-6

Dates: Created 2009/08/07; Completed 2009/08/20;

PMID: 19661432, status: MEDLINE (last retrieval date: 8/21/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

Comments and Corrections

CommentIn: Science. 2009 Aug 7;325(5941):684-5. (PMID: 19661407)

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

ATP-Dependent Proteases - metabolism
Anti-Bacterial Agents - pharmacology
Bacterial Outer Membrane Proteins - genetics; metabolism
Chloramphenicol - pharmacology
Escherichia coli - drug effects; genetics; metabolism
Escherichia coli Proteins - genetics; metabolism
Heat-Shock Proteins - genetics; metabolism
Membrane Proteins - genetics; metabolism
Mutant Proteins - metabolism

Periplasmic Proteins - genetics; metabolism
Porins - genetics; metabolism
Protein Sorting Signals
Protein Transport - drug effects
Receptors, Virus - genetics; metabolism
Recombinant Fusion Proteins - metabolism
Serine Endopeptidases - genetics; metabolism
Tetracycline - pharmacology
beta-Galactosidase - genetics; metabolism

Associated Chemicals: Anti-Bacterial Agents (0) ; Bacterial Outer Membrane Proteins (0) ; Escherichia coli Proteins (0) ; Heat-Shock Proteins (0) ; Membrane Proteins (0) ; Mutant Proteins (0) ; Periplasmic Proteins (0) ; Porins (0) ; Protein Sorting Signals (0) ; Receptors, Virus (0) ; Recombinant Fusion Proteins (0) ; SecY protein, E coli (0) ; YccA protein, E coli (0) ; maltoporins (0) ; Chloramphenicol (56-75-7) ; Tetracycline (60-54-8) ; beta-Galactosidase (EC 3.2.1.23) ; ATP-Dependent Proteases (EC 3.4.21.-) ; DegP protease (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; FtsH protein, E coli (EC 3.4.24.-)

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