{"title":"Min protein patterns emerge from rapid rebinding and membrane interaction of MinE","date_created":"2018-12-11T11:55:03Z","date_updated":"2021-01-12T06:54:31Z","author":[{"full_name":"Martin Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Elisabeth","last_name":"Fischer Friedrich","full_name":"Fischer-Friedrich, Elisabeth"},{"full_name":"Herold, Christoph","last_name":"Herold","first_name":"Christoph"},{"last_name":"Kruse","first_name":"Karsten","full_name":"Kruse, Karsten"},{"first_name":"Petra","last_name":"Schwille","full_name":"Schwille, Petra "}],"intvolume":"        18","doi":"10.1038/nsmb.2037","quality_controlled":0,"year":"2011","day":"01","_id":"1985","page":"577 - 583","issue":"5","publication":"Nature Structural and Molecular Biology","month":"05","citation":{"short":"M. Loose, E. Fischer Friedrich, C. Herold, K. Kruse, P. Schwille, Nature Structural and Molecular Biology 18 (2011) 577–583.","ieee":"M. Loose, E. Fischer Friedrich, C. Herold, K. Kruse, and P. Schwille, “Min protein patterns emerge from rapid rebinding and membrane interaction of MinE,” <i>Nature Structural and Molecular Biology</i>, vol. 18, no. 5. Nature Publishing Group, pp. 577–583, 2011.","apa":"Loose, M., Fischer Friedrich, E., Herold, C., Kruse, K., &#38; Schwille, P. (2011). Min protein patterns emerge from rapid rebinding and membrane interaction of MinE. <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nsmb.2037\">https://doi.org/10.1038/nsmb.2037</a>","ama":"Loose M, Fischer Friedrich E, Herold C, Kruse K, Schwille P. Min protein patterns emerge from rapid rebinding and membrane interaction of MinE. <i>Nature Structural and Molecular Biology</i>. 2011;18(5):577-583. doi:<a href=\"https://doi.org/10.1038/nsmb.2037\">10.1038/nsmb.2037</a>","chicago":"Loose, Martin, Elisabeth Fischer Friedrich, Christoph Herold, Karsten Kruse, and Petra Schwille. “Min Protein Patterns Emerge from Rapid Rebinding and Membrane Interaction of MinE.” <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group, 2011. <a href=\"https://doi.org/10.1038/nsmb.2037\">https://doi.org/10.1038/nsmb.2037</a>.","mla":"Loose, Martin, et al. “Min Protein Patterns Emerge from Rapid Rebinding and Membrane Interaction of MinE.” <i>Nature Structural and Molecular Biology</i>, vol. 18, no. 5, Nature Publishing Group, 2011, pp. 577–83, doi:<a href=\"https://doi.org/10.1038/nsmb.2037\">10.1038/nsmb.2037</a>.","ista":"Loose M, Fischer Friedrich E, Herold C, Kruse K, Schwille P. 2011. Min protein patterns emerge from rapid rebinding and membrane interaction of MinE. Nature Structural and Molecular Biology. 18(5), 577–583."},"publisher":"Nature Publishing Group","volume":18,"extern":1,"publication_status":"published","type":"journal_article","publist_id":"5098","acknowledgement":"This work was also supported by the Max Planck Society (M.L., E.F.-F., P.S.).","date_published":"2011-05-01T00:00:00Z","status":"public","abstract":[{"lang":"eng","text":"\n\nIn Escherichia coli, the pole-to-pole oscillation of the Min proteins directs septum formation to midcell, which is required for symmetric cell division. In vitro, protein waves emerge from the self-organization of MinD, a membrane-binding ATPase, and its activator MinE. For wave propagation, the proteins need to cycle through states of collective membrane binding and unbinding. Although MinD presumably undergoes cooperative membrane attachment, it is unclear how synchronous detachment is coordinated. We used confocal and single-molecule microscopy to elucidate the order of events during Min wave propagation. We propose that protein detachment at the rear of the wave, and the formation of the E-ring, are accomplished by two complementary processes: first, local accumulation of MinE due to rapid rebinding, leading to dynamic instability; and second, a structural change induced by membrane-interaction of MinE in an equimolar MinD-MinE (MinDE) complex, which supports the robustness of pattern formation."}]}