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Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation.
Bonny, Mike; Fischer-Friedrich, Elisabeth; Loose, Martin; Schwille, Petra; Kruse, Karsten.
Afiliação
  • Bonny M; Theoretische Physik, Universität des Saarlandes, Saarbrücken, Germany.
PLoS Comput Biol ; 9(12): e1003347, 2013.
Article em En | MEDLINE | ID: mdl-24339757
The rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior, which emerges from the interaction of the ATPase MinD and its activator MinE on the cell membrane, has become a paradigm for protein self-organization. Recently, it has been found that not only the binding of MinD to the membrane, but also interactions of MinE with the membrane contribute to Min-protein self-organization. Here, we show that by accounting for this finding in a computational model, we can comprehensively describe all observed Min-protein patterns in vivo and in vitro. Furthermore, by varying the system's geometry, our computations predict patterns that have not yet been reported. We confirm these predictions experimentally.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Ciclo Celular / Proteínas de Escherichia coli Tipo de estudo: Prognostic_studies Idioma: En Revista: PLoS Comput Biol Assunto da revista: BIOLOGIA / INFORMATICA MEDICA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Ciclo Celular / Proteínas de Escherichia coli Tipo de estudo: Prognostic_studies Idioma: En Revista: PLoS Comput Biol Assunto da revista: BIOLOGIA / INFORMATICA MEDICA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Alemanha