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10.1073/pnas.1509557112

http://scihub22266oqcxt.onion/10.1073/pnas.1509557112
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suck abstract from ncbi


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pmid26644587
      Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (51 ): 15725-30
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  • Supramolecular structure in the membrane of Staphylococcus aureus #MMPMID26644587
  • García-Lara J ; Weihs F ; Ma X ; Walker L ; Chaudhuri RR ; Kasturiarachchi J ; Crossley H ; Golestanian R ; Foster SJ
  • Proc Natl Acad Sci U S A 2015[Dec]; 112 (51 ): 15725-30 PMID26644587 show ga
  • 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.
  • |Bacterial Proteins/analysis [MESH]
  • |Cell Membrane/*ultrastructure [MESH]
  • |Entropy [MESH]
  • |Lipid Metabolism [MESH]


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