Single channel activity of OmpF-like porin from Yersinia pseudotuberculosis
| Autor: | Gennadiy A. Naberezhnykh, V. I. Gorbach, Yuri N. Antonenko, Elena A. Kotova, Elena Zelepuga, Alexander M. Firsov, V. A. Khomenko, Olga D. Novikova, Tatyana I. Rokitskaya |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lipid Bilayers Biophysics Porins medicine.disease_cause Biochemistry Ion Channels Membrane Potentials 03 medical and health sciences Escherichia coli medicine Yersinia pseudotuberculosis Lipid bilayer Ion channel Membrane potential Liposome 030102 biochemistry & molecular biology biology Chemistry Cell Biology Hydrogen-Ion Concentration biology.organism_classification 030104 developmental biology Membrane Porin bacteria Bacterial Outer Membrane Proteins |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1858:883-891 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2016.02.005 |
| Popis: | To gain a mechanistic insight in the functioning of the OmpF-like porin from Yersinia pseudotuberculosis (YOmpF), we compared the effect of pH variation on the ion channel activity of the protein in planar lipid bilayers and its binding to lipid membranes. The behavior of YOmpF channels upon acidification was similar to that previously described for Escherichia coli OmpF. In particular, a decrease in pH of the bathing solution resulted in a substantial reduction of YOmpF single channel conductance, accompanied by the emergence of subconductance states. Similar subconductance substates were elicited by the addition of lysophosphatidylcholine. This observation, made with porin channels for the first time, pointed to the relevance of lipid-protein interactions, in particular, the lipid curvature stress, to the appearance of subconductance states at acidic pH. Binding of YOmpF to membranes displayed rather modest dependence on pH, whereas the channel-forming potency of the protein tremendously decreased upon acidification. |
| Databáze: | OpenAIRE |
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