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The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways

The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways

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POCANSCHI, Cosmin L., Hans-Jürgen APELL, Pål PUNTERVOLL, Bente HØGH, Harald B. JENSEN, Wolfram WELTE, Jörg H. KLEINSCHMIDT, 2006. The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways. In: Journal of Molecular Biology. 355(3), pp. 548-561. ISSN 0022-2836. eISSN 1089-8638

@article{Pocanschi2006major-8581, title={The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways}, year={2006}, number={3}, volume={355}, issn={0022-2836}, journal={Journal of Molecular Biology}, pages={548--561}, author={Pocanschi, Cosmin L. and Apell, Hans-Jürgen and Puntervoll, Pål and Høgh, Bente and Jensen, Harald B. and Welte, Wolfram and Kleinschmidt, Jörg H.} }

The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways Kleinschmidt, Jörg H. Puntervoll, Pål Kleinschmidt, Jörg H. Pocanschi, Cosmin L. 2006 Jensen, Harald B. Høgh, Bente 2011-03-24T17:44:51Z Høgh, Bente Jensen, Harald B. application/pdf Puntervoll, Pål Apell, Hans-Jürgen Membrane protein insertion and folding was studied for the major outer membrane protein of Fusobacterium nucleatum (FomA), which is a voltagedependent general diffusion porin. The transmembrane domain of FomA forms a b-barrel that is predicted to consist of 14 b-strands. Here, unfolded FomA is shown to insert and fold spontaneously and quantitatively into phospholipid bilayers upon dilution of the denaturant urea, which was shown previously only for outer membrane protein A (OmpA) of Escherichia coli. Folding of FomA is demonstrated by circular dichroism and fluorescence spectroscopy, by SDS-polyacrylamide gel electrophoresis, and by single-channel recordings. Refolded FomA had a single-channel conductance of 1.1 nS at 1 M KCl, in agreement with the conductance of FomA isolated from membranes in native form. In contrast to OmpA, which forms a smaller eight-stranded b-barrel domain, folding kinetics of the larger FomA were slower and provided evidence for parallel folding pathways of FomA into lipid bilayers. Two pathways were observed independent of membrane thickness with two different lipid bilayers, which were either composed of dicapryl phosphatidylcholine or dioleoyl phosphatidylcholine. This is the first observation of parallel membrane insertion and folding pathways of a b-barrel membrane protein from an unfolded state in urea into lipid bilayers. The kinetics of both folding pathways depended on the chain length of the lipid and on temperature with estimated activation energies of 19 kJ/mol (dicapryl phosphatidylcholine) and 70 kJ/mol (dioleoyl phosphatidylcholine) for the faster<br />pathways. eng 2011-03-24T17:44:51Z Apell, Hans-Jürgen Welte, Wolfram Pocanschi, Cosmin L. First publ. in: Journal of Molecular Biology 355 (2006), pp. 548-561 Welte, Wolfram deposit-license

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