Directionality of substrate translocation of the hemolysin A Type I secretion System
| Autor: | Lutz Schmitt, Sander H. J. Smits, Stefanie Weidtkamp-Peters, Diana Kleinschrodt, Karl-Erich Jaeger, Michael H. H. Lenders |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Genetics
Proteases Multidisciplinary Escherichia coli Proteins Hemolysin Biology biology.organism_classification medicine.disease_cause Corrigenda Article Green fluorescent protein Cell biology Hemolysin Proteins Protein Transport Membrane protein complex Escherichia coli Protein Translocation Systems Extracellular medicine ddc:000 Secretion Bacteria |
| Zdroj: | Scientific reports 5, 12470 (2015). doi:10.1038/srep12470 Scientific Reports |
| DOI: | 10.1038/srep12470 |
| Popis: | Type 1 secretion systems (T1SS) of Gram-negative bacteria are responsible for the secretion of various proteases, lipases, S-layer proteins or toxins into the extracellular space. The paradigm of these systems is the hemolysin A (HlyA) T1SS of Escherichia coli. This multiple membrane protein complex is able to secrete the toxin HlyA in one step across both E. coli membranes. Common to all secreted T1SS substrates is a C-terminal secretion sequence being necessary as well as sufficient for secretion. However, it is not known whether transport occurs directionally, i.e. the N- or the C-terminus of T1SS substrates is secreted first. We have addressed this question by constructing HlyA fusions with the rapidly folding eGFP resulting in a stalled T1SS. Differential labeling and subsequent fluorescence microscopic detection of C- and N-terminal parts of the fusions allowed us to demonstrate vectorial transport of HlyA through the T1SS with the C-terminus appearing first outside the bacterial cells. |
| Databáze: | OpenAIRE |
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