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Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin
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P13 is one of the major outer membrane proteins of Borrelia burgdorferi. Previous studies described P13 as a porin. In the present study some structure and function aspects of P13 were studied. P13 showed according to lipid bilayer studies a channel-forming activity of 0.6 nanosiemens in 1 m KCl. Single channel and selectivity measurements demonstrated that P13 had no preference for either cations or anions and showed no voltage-gating up to ±100 mV. Blue native polyacrylamide gel electrophoresis was used to isolate and characterize the P13 protein complex in its native state. The complex had a high molecular mass of about 300 kDa and was only composed of P13 monomers. The channel size was investigated using non-electrolytes revealing an apparent diameter of about 1.4 nm with a 400-Da molecular mass cut-off. Multichannel titrations with different substrates reinforced the idea that P13 forms a general diffusion channel. The identity of P13 within the complex was confirmed by second dimension SDS-PAGE, Western blotting, mass spectrometry, and the use of a p13 deletion mutant strain. The results suggested that P13 is the protein responsible for the 0.6-nanosiemens pore-forming activity in the outer membrane of B. burgdorferi.
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BÁRCENA URIBARRI, Iván, et al. Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin. Journal of Biological Chemistry. 2014. Vol. 289, núm. 27, pàgs. 18614-18624. ISSN 0021-9258. [consulta: 8 de maig de 2026]. Disponible a: https://hdl.handle.net/2445/177357