| Spatial regulators for bacterial cell division self-organize into surface waves in vitro. | |
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MedLine Citation:
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PMID: 18467587 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In the bacterium Escherichia coli, the Min proteins oscillate between the cell poles to select the cell center as division site. This dynamic pattern has been proposed to arise by self-organization of these proteins, and several models have suggested a reaction-diffusion type mechanism. Here, we found that the Min proteins spontaneously formed planar surface waves on a flat membrane in vitro. The formation and maintenance of these patterns, which extended for hundreds of micrometers, required adenosine 5'-triphosphate (ATP), and they persisted for hours. We present a reaction-diffusion model of the MinD and MinE dynamics that accounts for our experimental observations and also captures the in vivo oscillations. |
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Authors:
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Martin Loose; Elisabeth Fischer-Friedrich; Jonas Ries; Karsten Kruse; Petra Schwille |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Science (New York, N.Y.) Volume: 320 ISSN: 1095-9203 ISO Abbreviation: Science Publication Date: 2008 May |
Date Detail:
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Created Date: 2008-05-09 Completed Date: 2008-05-23 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0404511 Medline TA: Science Country: United States |
Other Details:
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Languages: eng Pagination: 789-92 Citation Subset: IM |
Affiliation:
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Biotechnologisches Zentrum der Technischen Universität Dresden, Tatzberg 47-51, 01307 Dresden, Germany. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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physiology* Adenosine Triphosphate / physiology Bacterial Proteins Cell Cycle Proteins / physiology* Cell Division / physiology* Cell-Free System Cytoskeletal Proteins Diffusion Escherichia coli / physiology* Escherichia coli Proteins / physiology* Models, Biological Oscillometry |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Cell Cycle Proteins; 0/Cytoskeletal Proteins; 0/Escherichia coli Proteins; 0/FtsZ protein, Bacteria; 0/MinE protein, E coli; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/MinD protein, E coli |
| Comments/Corrections | |
Comment In:
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Science. 2008 May 9;320(5877):755-6
[PMID:
18467579
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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