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  Study of the Protein Complex, Pore Diameter, and Pore-forming Activity of the Borrelia burgdorferi P13 Porin

Barcena-Uribarri, I., Thein, M., Barbot, M., Sans-Serramitjana, E., Bonde, M., Mentele, R., et al. (2014). Study of the Protein Complex, Pore Diameter, and Pore-forming Activity of the Borrelia burgdorferi P13 Porin. JOURNAL OF BIOLOGICAL CHEMISTRY, 289(27), 18614-18624. doi:10.1074/jbc.M113.539528.

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 Creators:
Barcena-Uribarri, Ivan1, Author
Thein, Marcus1, Author
Barbot, Mariam1, Author
Sans-Serramitjana, Eulalia1, Author
Bonde, Mari1, Author
Mentele, Reinhard2, Author           
Lottspeich, Friedrich2, Author           
Bergstrom, Sven1, Author
Benz, Roland1, Author
Affiliations:
1external, ou_persistent22              
2Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

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Free keywords: LIPID BILAYER-MEMBRANES; LYME-DISEASE SPIROCHETE; COLI OUTER-MEMBRANE; ESCHERICHIA-COLI; BINDING-SITE; INSERTIONAL INACTIVATION; MOLECULAR-BASIS; ION CHANNELS; PERMEABILITY; ELIMINATION
 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.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000339062900001
DOI: 10.1074/jbc.M113.539528
 Degree: -

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Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 289 (27) Sequence Number: - Start / End Page: 18614 - 18624 Identifier: ISSN: 0021-9258