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Curr Opin Struct Biol. 2015 Dec;35:109-15. doi: 10.1016/j.sbi.2015.10.007. Epub 2015 Nov 26.

Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.

Author information

1
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: colin.kleanthous@bioch.ox.ac.uk.
2
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
3
Department of Biology, University of York, York YO10 5DD, UK. Electronic address: christoph.baumann@york.ac.uk.

Abstract

It has until recently been unclear whether outer membrane proteins (OMPs) of Gram-negative bacteria are organized or distributed randomly. Studies now suggest promiscuous protein-protein interactions (PPIs) between β-barrel OMPs in Escherichia coli govern their local and global dynamics, engender spatiotemporal patterning of the outer membrane into micro-domains and are the basis of β-barrel protein turnover. We contextualize these latest advances, speculate on areas of bacterial cell biology that might be influenced by the organization of OMPs into supramolecular assemblies, and highlight the new questions and controversies this revised view of the bacterial outer membrane raises.

PMID:
26629934
PMCID:
PMC4684144
DOI:
10.1016/j.sbi.2015.10.007
[Indexed for MEDLINE]
Free PMC Article

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