The TatAd component of the Bacillus subtilis twin-arginine protein transport system forms homo-multimeric complexes in its cytosolic and membrane embedded localisation
| Autor: | Sandra Schreiber, Ovidiu I. Pop, Thomas Raul Appel, Martin Westermann, Wiebke Schlörmann, Jörg P. Müller, Roman G. Gerlach |
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| Rok vydání: | 2006 |
| Předmět: |
biology
Macromolecular Substances Protein export Cell Membrane Biophysics Membrane Transport Proteins Complex formation Bacillus subtilis Immunogold labelling Cell Biology biology.organism_classification Biochemistry Transport protein Chloroplast Cytosol Membrane Bacterial Proteins Cytoplasm Thylakoid Twin-arginine translocation Freeze Fracturing TatA |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1758(4):443-451 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2006.03.018 |
| Popis: | The twin arginine translocation (Tat) system has the capacity to transfer completely folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. The most abundant TatA protein of this system has been suggested to form the protein conducting channel. Here, the molecular organisation of soluble and membrane embedded Bacillus subtilis TatAd was analysed using negative contrast and freeze-fractured electron microscopy. In both compartments, the protein showed homo-oligomerisation. In aqueous solution, TatAd formed homo-multimeric micelle-like complexes. Freeze-fracture analysis of proteoliposomes revealed self association of membrane-integrated TatAd independent from TatCd, the second component of this transport system. Immunogold labelling demonstrated that the substrate prePhoD was co-localised with membrane-integrated TatAd complexes. |
| Databáze: | OpenAIRE |
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