title: Supramolecular structure in the membrane of Staphylococcus aureus.
abstract: All life demands the temporal and spatial control of essential biological functions. In bacteria, the recent discovery of coordinating elements provides a framework to begin to explain cell growth and division. Here we present the discovery of a supramolecular structure in the membrane of the coccal bacterium Staphylococcus aureus, which leads to the formation of a large-scale pattern across the entire cell body; this has been unveiled by studying the distribution of essential proteins involved in lipid metabolism (PlsY and CdsA). The organization is found to require MreD, which determines morphology in rod-shaped cells. The distribution of protein complexes can be explained as a spontaneous pattern formation arising from the competition between the energy cost of bending that they impose on the membrane, their entropy of mixing, and the geometric constraints in the system. Our results provide evidence for the existence of a self-organized and nonpercolating molecular scaffold involving MreD as an organizer for optimal cell function and growth based on the intrinsic self-assembling properties of biological molecules.
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Jorge
authors.initials: J
authors.lastname: García-Lara
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Felix
authors.initials: F
authors.lastname: Weihs
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Xing
authors.initials: X
authors.lastname: Ma
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Lucas
authors.initials: L
authors.lastname: Walker
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Roy R
authors.initials: RR
authors.lastname: Chaudhuri
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Jagath
authors.initials: J
authors.lastname: Kasturiarachchi
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom;
authors.forename: Howard
authors.initials: H
authors.lastname: Crossley
authors.affiliation: Rudolf Peierls Centre for Theoretical Physics, University of Oxford, Oxford OX1 3NP, United Kingdom s.foster@sheffield.ac.uk ramin.golestanian@physics.ox.ac.uk.
authors.forename: Ramin
authors.initials: R
authors.lastname: Golestanian
authors.affiliation: The Krebs Institute, Department of Molecular Biology and Microbiology, University of Sheffield, Sheffield S10 2TN, United Kingdom; s.foster@sheffield.ac.uk ramin.golestanian@physics.ox.ac.uk.
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Foster
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis; D002462:Cell Membrane / Q000648:ultrastructure*; D019277:Entropy; D050356:Lipid Metabolism; D013211:Staphylococcus aureus / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D001426:Bacterial Proteins
keywords: MreD; PlsY; membrane; model; staphylococcus