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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1999-11-8
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pubmed:abstractText |
By inhibiting FtsZ ring formation near the cell ends, the MinC protein plays a critical role in proper positioning of the division apparatus in Escherichia coli. MinC activity requires that of MinD, and the MinE peptide provides topological specificity by suppressing MinC-MinD-mediated division inhibition specifically at the middle of the cell. We recently presented evidence that MinE not only accumulates in an FtsZ-independent ring structure at the cell's middle but also imposes a unique dynamic localization pattern upon MinD in which the latter accumulates alternately in either one of the cell halves in what appears to be a rapidly oscillating membrane association-dissociation cycle. Here we show that functional green fluorescent protein-MinC displays a very similar oscillatory behavior which is dependent on both MinD and MinE and independent of FtsZ. The results support a model in which MinD recruits MinC to its site of action and in which FtsZ ring assembly at each of the cell ends is blocked in an intermittent and alternate fashion.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-10074085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-10220403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-10231488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-10339512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-1406249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-16591472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-1729224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-1836760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-1925029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2137246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2183010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2188963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2194248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2645057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2666394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-2834323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-3330757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-4597442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-4939776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-7567988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-7726836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-8432706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-8707053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-8709851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-8752322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-8830694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9054497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9068638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9219999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9242903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9393861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-94144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9442879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9501185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9529889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9675800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9683493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9720867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9808628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9811667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10515933-9829948
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsZ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MinC protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/MinD protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/MinE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6419-24
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:10515933-Adenosine Triphosphatases,
pubmed-meshheading:10515933-Bacterial Proteins,
pubmed-meshheading:10515933-Cell Compartmentation,
pubmed-meshheading:10515933-Cell Cycle Proteins,
pubmed-meshheading:10515933-Cell Division,
pubmed-meshheading:10515933-Cytoskeletal Proteins,
pubmed-meshheading:10515933-Escherichia coli,
pubmed-meshheading:10515933-Escherichia coli Proteins,
pubmed-meshheading:10515933-Green Fluorescent Proteins,
pubmed-meshheading:10515933-Growth Inhibitors,
pubmed-meshheading:10515933-Luminescent Proteins,
pubmed-meshheading:10515933-Models, Biological,
pubmed-meshheading:10515933-Periodicity,
pubmed-meshheading:10515933-Recombinant Fusion Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli.
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pubmed:affiliation |
Department of Molecular Biology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106-4960, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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