Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria

Patrice Rassam, Nikki A. Copeland, Oliver Birkholz, Csaba Tóth, Matthieu Chavent, Anna L. Duncan, Stephen J. Cross, Nicholas G. Housden, Renata Kaminska, Urban Seger, Diana M. Quinn, Tamsin J. Garrod, Mark S. P. Sansom, Jacob Piehler, Christoph G. Baumann () and Colin Kleanthous ()
Additional contact information
Patrice Rassam: University of Oxford
Nikki A. Copeland: University of York
Oliver Birkholz: University of Osnabrück
Csaba Tóth: University of York
Matthieu Chavent: University of Oxford
Anna L. Duncan: University of Oxford
Stephen J. Cross: University of York
Nicholas G. Housden: University of Oxford
Renata Kaminska: University of Oxford
Urban Seger: University of York
Diana M. Quinn: University of York
Tamsin J. Garrod: University of York
Mark S. P. Sansom: University of Oxford
Jacob Piehler: University of Osnabrück
Christoph G. Baumann: University of York
Colin Kleanthous: University of Oxford

Nature, 2015, vol. 523, issue 7560, 333-336

Abstract: Fluorescent labelling is used to show that in E. coli, outer membrane protein (OMP) turnover is passive and binary in nature, and OMPs cluster to form islands in which diffusion of individual proteins is restricted owing to lateral interactions with other OMPs; new OMPs are inserted mostly at mid-cell, meaning that old OMP islands are displaced to the poles of growing cells.

Date: 2015
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DOI: 10.1038/nature14461

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