Sökning: onr:"swepub:oai:DiVA.org:umu-91837" >
Study of the protei...
Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin
-
Bárcena-Uribarri, Iván (författare)
-
Thein, Marcus (författare)
-
Barbot, Mariam (författare)
-
visa fler...
-
Sans-Serramitjana, Eulalia (författare)
-
- Bonde, Mari (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
-
Mentele, Reinhard (författare)
-
Lottspeich, Friedrich (författare)
-
- Bergström, Sven (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
-
Benz, Roland (författare)
-
visa färre...
-
(creator_code:org_t)
- American Society for Biochemistry and Molecular Biology, 2014
- 2014
- Engelska.
-
Ingår i: Journal of Biological Chemistry. - : American Society for Biochemistry and Molecular Biology. - 0021-9258 .- 1083-351X. ; 289:27, s. 18614-18624
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas