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

Date publication

décembre 2015

Journal

Current opinion in structural biology

Auteurs

Membres identifiés du Cancéropôle Est :
Dr RASSAM Patrice

Tous les auteurs :
Kleanthous C, Rassam P, Baumann CG

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/26629934

Résumé

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.

Mots clés

Bacterial Outer Membrane Proteins, metabolism, Cell Membrane, metabolism, Gram-Negative Bacteria, cytology, Protein Interaction Mapping, methods, Spatio-Temporal Analysis, Substrate Specificity

Référence

Curr Opin Struct Biol. 2015 12;35:109-15