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Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis

MPG-Autoren

Kozjak-Pavlovic,  Vera
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81971

Kepp,  Oliver
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons82127

Ross,  Katharina
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons82110

Rajalingam,  Krishnaraj
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81924

Harsman,  Anke
Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81926

Hauf,  Eva
Core Facilities / Microscopy, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81827

Brinkmann,  Volker
Core Facilities / Microscopy, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81909

Günther,  Dirk
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81933

Herrmann,  Ines
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons81946

Hurwitz,  Robert
Core Facilities / Proteinpurification, Max Planck Institute for Infection Biology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons82130

Rudel,  Thomas
Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society;

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PLoS_Pathogens_2009_5_e1000629.pdf
(Verlagsversion), 912KB

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Zitation

Kozjak-Pavlovic, V., Dian-Lothrop, E. A., Meinecke, M., Kepp, O., Ross, K., Rajalingam, K., et al. (2009). Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis. PLoS Pathogens, 5(10): e1000629.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-000E-C094-9
Zusammenfassung
The bacterial PorB porin, an ATP-binding beta-barrel protein of pathogenic Neisseria gonorrhoeae, triggers host cell apoptosis by an unknown mechanism. PorB is targeted to and imported by host cell mitochondria, causing the breakdown of the mitochondrial membrane potential (Delta psi(m)). Here, we show that PorB induces the condensation of the mitochondrial matrix and the loss of cristae structures, sensitizing cells to the induction of apoptosis via signaling pathways activated by BH3-only proteins. PorB is imported into mitochondria through the general translocase TOM but, unexpectedly, is not recognized by the SAM sorting machinery, usually required for the assembly of beta-barrel proteins in the mitochondrial outer membrane. PorB integrates into the mitochondrial inner membrane, leading to the breakdown of Delta psi(m). The PorB channel is regulated by nucleotides and an isogenic PorB mutant defective in ATP-binding failed to induce Delta psi(m) loss and apoptosis, demonstrating that dissipation of Delta psi(m) is a requirement for cell death caused by neisserial infection.