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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2007-6-4
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pubmed:abstractText |
The F plasmid is actively partitioned to daughter cells by the sopABC gene. To elucidate the partitioning mechanisms, we simultaneously analysed movements of the plasmid and the SopA ATPase in single living cells. SopA, which is a putative motor protein assembled densely near nucleoid borders and formed a single discrete focus associated with less dense filamentous distribution along the long axis of the cell. The dense SopA focus oscillates between cell poles. The direction of the plasmid motion switches as the SopA focus switches its position. The velocity of the plasmid motion stays constant while it oscillates moving towards the SopA focus. The low density filamentous distribution of SopA persisted throughout the SopA oscillation. The focus associated with filamentous distribution of SopA was also observed in a cell without nucleoid. The SopA filament may guide the movement of the plasmid as a railway track and lead it to cell quarters.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10220403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10619014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10619015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10652275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10811905,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-10931339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-11018141,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17542915-9915704
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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/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SopA protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/SopB protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1198-213
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17542915-Adenosine Triphosphatases,
pubmed-meshheading:17542915-Bacterial Proteins,
pubmed-meshheading:17542915-Cell Nucleus,
pubmed-meshheading:17542915-DNA, Bacterial,
pubmed-meshheading:17542915-Escherichia coli,
pubmed-meshheading:17542915-Escherichia coli Proteins,
pubmed-meshheading:17542915-F Factor,
pubmed-meshheading:17542915-Green Fluorescent Proteins,
pubmed-meshheading:17542915-Kinetics,
pubmed-meshheading:17542915-Models, Biological,
pubmed-meshheading:17542915-Recombinant Fusion Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Oscillating focus of SopA associated with filamentous structure guides partitioning of F plasmid.
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pubmed:affiliation |
Microbial Genetics Laboratory, Genetic Strains Research Center, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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