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  Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

Norell, D., Heuck, A., Tran-Thi, T.-A., Götzke, H., Jacob-Dubuisson, F., Clausen, T., et al. (2014). Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins. Nature Communications, 5: 5396. doi:10.1038/ncomms6396.

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Norell, D, Autor
Heuck, A, Autor
Tran-Thi, T-A, Autor
Götzke, H, Autor
Jacob-Dubuisson, F, Autor
Clausen, T, Autor
Daley, DO, Autor
Braun, V1, Autor           
Müller, M, Autor
Fan, E, Autor
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              

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 Zusammenfassung: Gram-negative bacteria use the type-V secretion pathway to expose proteins at their cell surface, many of which have virulence functions. Translocation of those proteins across the outer membrane occurs either by means of dedicated translocator proteins (two-partner secretion) or covalently fused translocator domains (autotransporters). Translocator proteins and translocator domains are β-barrels requiring the β-barrel assembly machinery (BAM) for membrane integration. However, the molecular details of their passage across the envelope and insertion into the outer membrane remain enigmatic, owing in part to the fact that in vitro systems are not available. Here we describe a versatile in vitro reconstitution system that faithfully reproduces both branches of the type-V secretion pathway and the assembly of β-barrel outer membrane proteins. This system will allow an in-depth analysis of protein secretion across and integration into outer membranes.

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 Datum: 2014-11
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1038/ncomms6396
PMID: 25369922
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Titel: Nature Communications
  Kurztitel : Nat. Commun.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: 9 Band / Heft: 5 Artikelnummer: 5396 Start- / Endseite: - Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723