title: Single channel activity of OmpF-like porin from Yersinia pseudotuberculosis.
abstract: 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.
authors: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow 119991, Russia.
authors: Tatyana I
authors: TI
authors: Rokitskaya
authors: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow 119991, Russia.
authors: Elena A
authors: EA
authors: Kotova
authors: Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Prospect 100 let Vladivostoku 159, Vladivostok 690022, Russia.
authors: Gennadiy A
authors: GA
authors: Naberezhnykh
authors: Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Prospect 100 let Vladivostoku 159, Vladivostok 690022, Russia.
authors: Valentina A
authors: VA
authors: Khomenko
authors: Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Prospect 100 let Vladivostoku 159, Vladivostok 690022, Russia.
authors: Vladimir I
authors: VI
authors: Gorbach
authors: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow 119991, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Leninskie Gory 1/73, Moscow 119991, Russia.
authors: Alexander M
authors: AM
authors: Firsov
authors: Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Prospect 100 let Vladivostoku 159, Vladivostok 690022, Russia.
authors: Elena A
authors: EA
authors: Zelepuga
authors: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow 119991, Russia. Electronic address: antonen@genebee.msu.ru.
authors: Yuri N
authors: YN
authors: Antonenko
authors: Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Prospect 100 let Vladivostoku 159, Vladivostok 690022, Russia. Electronic address: novolga_05@mail.ru.
authors: Olga D
authors: OD
authors: Novikova
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli; D006863:Hydrogen-Ion Concentration; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry*; D008564:Membrane Potentials; D018272:Porins / Q000737:chemistry* / Q000378:metabolism; D015011:Yersinia pseudotuberculosis
chemical_list: D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; C109237:OmpF protein; D018272:Porins
keywords: Bacterial porin; Ion channel; Ionic current; Liposome; Lysophosphatidylcholine; Outer membrane protein; Planar bilayer lipid membrane; pH dependence