Dynamics of Unfolded Protein Transport through an Aerolysin Pore
| Autor: | Françoise Gisou van der Goot, Juan Pelta, Leila Rabah, Jean-Michel Betton, Bénédicte Thiebot, Manuela Pastoriza-Gallego, Gabriel Gibrat, Loïc Auvray |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Pore Forming Cytotoxic Proteins
Bacterial Toxins Aerolysin 02 engineering and technology 010402 general chemistry 01 natural sciences Biochemistry Catalysis Maltose-binding protein Colloid and Surface Chemistry Electricity Escherichia coli Protein Unfolding biology Membrane transport protein DNA transport Chemistry Escherichia coli Proteins General Chemistry 021001 nanoscience & nanotechnology Recombinant Proteins 0104 chemical sciences Transport protein Protein Transport Nanopore Crystallography Periplasmic Binding Proteins Mutation biology.protein Biophysics Unfolded protein response Protein folding 0210 nano-technology |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja1073245 |
| Popis: | Protein export is an essential mechanism in living cells and exported proteins are usually translocated through a protein-conducting channel in an unfolded state. Here we analyze, by electrical detection, the entry and transport of unfolded proteins, at the single molecule level, with different stabilities through an aerolysin pore, as a function of the applied voltage and protein concentration. The frequency of ionic current blockades varies exponentially as a function of the applied voltage and linearly as a function of protein concentration. The transport time of unfolded proteins decreases exponentially when the applied voltage increases. We prove that the ionic current blockade duration of a double-sized protein is longer than that assessed for a single protein supporting the transport phenomenon. Our results fit with the theory of confined polyelectrolyte and with some experimental results about DNA or synthetic polyelectrolyte translocation through protein channels as a function of applied voltage. We discuss the potential of the aerolysin nanopore as a tool for protein folding studies as it has already been done for α-hemolysin. |
| Databáze: | OpenAIRE |
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