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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0018270,
umls-concept:C0023175,
umls-concept:C0026882,
umls-concept:C0205145,
umls-concept:C0205307,
umls-concept:C0229992,
umls-concept:C0237477,
umls-concept:C0596901,
umls-concept:C0813983,
umls-concept:C1260969,
umls-concept:C1293097,
umls-concept:C1514562,
umls-concept:C1517945,
umls-concept:C1522492,
umls-concept:C1524072,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
13
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pubmed:dateCreated |
2002-7-2
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pubmed:abstractText |
The MinE protein functions as a topological specificity factor in determining the site of septal placement in Escherichia coli. MinE assembles into a membrane-associated ring structure near midcell and directs the localization of MinD and MinC into a membrane- associated polar zone that undergoes a characteristic pole-to-pole oscillation cycle. Single (green fluorescent protein) and double label (yellow fluorescent protein/cyan fluorescent protein) fluorescence labeling experiments showed that mutational alteration of a site on the alpha-face of MinE led to a failure to assemble the MinE ring, associated with loss of the ability to support a normal pattern of division site placement. The absence of the MinE ring did not prevent the assembly and disassembly of the MinD polar zone. Mutant cells lacking the MinE ring were characterized by the growth of MinD polar zones past their normal arrest point near midcell. The results suggested that the MinE ring acts as a stop-growth mechanism to prevent the MinCD polar zone from extending beyond the midcell division site.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10096083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10220403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10515933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10540287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10633093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-10690414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-11062554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-11158581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-11285221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-11430835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-1336094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-1836760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-1989883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-2645057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-7753804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-7809066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-8707053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-8709851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-9393861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-9759496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093736-9791172
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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/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
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,
http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3347-57
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12093736-Adenosine Triphosphatases,
pubmed-meshheading:12093736-Amino Acid Substitution,
pubmed-meshheading:12093736-Bacterial Proteins,
pubmed-meshheading:12093736-Cell Cycle Proteins,
pubmed-meshheading:12093736-Cell Membrane,
pubmed-meshheading:12093736-Cell Polarity,
pubmed-meshheading:12093736-Dimerization,
pubmed-meshheading:12093736-Escherichia coli,
pubmed-meshheading:12093736-Escherichia coli Proteins,
pubmed-meshheading:12093736-Genes, Reporter,
pubmed-meshheading:12093736-Green Fluorescent Proteins,
pubmed-meshheading:12093736-Luminescent Proteins,
pubmed-meshheading:12093736-Membrane Proteins,
pubmed-meshheading:12093736-Models, Molecular,
pubmed-meshheading:12093736-Mutagenesis, Site-Directed,
pubmed-meshheading:12093736-Phenotype,
pubmed-meshheading:12093736-Protein Conformation,
pubmed-meshheading:12093736-Recombinant Fusion Proteins,
pubmed-meshheading:12093736-Structure-Activity Relationship
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pubmed:year |
2002
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pubmed:articleTitle |
Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains.
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pubmed:affiliation |
Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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