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Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2014 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 5, 5396- p.Article in journal (Refereed) Published
Abstract [en]

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 beta-barrels requiring the beta-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 beta-barrel outer membrane proteins. This system will allow an in-depth analysis of protein secretion across and integration into outer membranes.

Place, publisher, year, edition, pages
2014. Vol. 5, 5396- p.
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Biological Sciences
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URN: urn:nbn:se:su:diva-111931DOI: 10.1038/ncomms6396ISI: 000345624800017OAI: oai:DiVA.org:su-111931DiVA: diva2:777249
Note

AuthorCount:10;

Available from: 2015-01-08 Created: 2015-01-08 Last updated: 2017-12-05Bibliographically approved

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