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http://hdl.handle.net/2445/177357
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DC Field | Value | Language |
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dc.contributor.author | Bárcena Uribarri, Iván | - |
dc.contributor.author | Thein, Marcus | - |
dc.contributor.author | Barbot, Mariam | - |
dc.contributor.author | Sans Serramitjana, Eulàlia | - |
dc.contributor.author | Bonde, Mari | - |
dc.contributor.author | Mentele, Reinhard | - |
dc.contributor.author | Lottspeich, Friedrich | - |
dc.contributor.author | Bergström, Sven | - |
dc.contributor.author | Benz, Roland | - |
dc.date.accessioned | 2021-05-18T10:21:27Z | - |
dc.date.available | 2021-05-18T10:21:27Z | - |
dc.date.issued | 2014-07-04 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/2445/177357 | - |
dc.description.abstract | 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. | - |
dc.format.extent | 11 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1074/jbc.M113.539528 | - |
dc.relation.ispartof | Journal of Biological Chemistry, 2014, vol. 289, num. 27, p. 18614-18624 | - |
dc.relation.uri | https://doi.org/10.1074/jbc.M113.539528 | - |
dc.rights | (c) American Society for Biochemistry and Molecular Biology, 2014 | - |
dc.source | Articles publicats en revistes (Patologia i Terapèutica Experimental) | - |
dc.subject.classification | Bacteris | - |
dc.subject.classification | Proteïnes | - |
dc.subject.classification | Química | - |
dc.subject.classification | Metabolisme | - |
dc.subject.other | Bacteria | - |
dc.subject.other | Proteins | - |
dc.subject.other | Chemistry | - |
dc.subject.other | Metabolism | - |
dc.title | Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 660906 | - |
dc.date.updated | 2021-05-18T10:21:27Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 24825899 | - |
Appears in Collections: | Articles publicats en revistes (Patologia i Terapèutica Experimental) |
Files in This Item:
File | Description | Size | Format | |
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660906.pdf | 963.99 kB | Adobe PDF | View/Open |
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