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

Colin Kleanthous; Patrice Rassam; Christoph G. Baumann

doi:10.1016/j.sbi.2015.10.007

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

Colin Kleanthous^*, Patrice Rassam, Christoph G. Baumann

^*Corresponding author for this work

University of York

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	109-115
Number of pages	7
Journal	CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume	35
DOIs	https://doi.org/10.1016/j.sbi.2015.10.007
Publication status	Published - 1 Dec 2015

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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.",

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AB - 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.

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JO - CURRENT OPINION IN STRUCTURAL BIOLOGY

JF - CURRENT OPINION IN STRUCTURAL BIOLOGY

ER -

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

Abstract

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