Source:http://linkedlifedata.com/resource/pubmed/id/17493130
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-5-11
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pubmed:abstractText |
The earliest event in bacterial cell division is the formation of a Z ring, composed of the tubulin-like FtsZ protein, at the division site at midcell. This ring then recruits several other division proteins and together they drive the formation of a division septum between two replicated chromosomes. Here we show that, in addition to forming a cytokinetic ring, FtsZ localizes in a helical-like pattern in vegetatively growing cells of Bacillus subtilis. FtsZ moves rapidly within this helix-like structure. Examination of FtsZ localization in individual live cells undergoing a single cell cycle suggests a new assembly mechanism for Z ring formation that involves a cell cycle-mediated multistep remodelling of FtsZ polymers. Our observations suggest that initially FtsZ localizes in a helical pattern, with movement of FtsZ within this structure occurring along the entire length of the cell. Next, movement of FtsZ in a helical-like pattern is restricted to a central region of the cell. Finally the FtsZ ring forms precisely at midcell. We further show that another division protein, FtsA, shown to interact with FtsZ prior to Z ring formation in B. subtilis, also localizes to similar helical patterns in vegetatively growing cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsA protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/FtsZ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0950-382X
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pubmed:author | |
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 |
487-99
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pubmed:meshHeading |
pubmed-meshheading:17493130-Bacillus subtilis,
pubmed-meshheading:17493130-Bacterial Proteins,
pubmed-meshheading:17493130-Cytokinesis,
pubmed-meshheading:17493130-Cytoskeletal Proteins,
pubmed-meshheading:17493130-Microbial Viability,
pubmed-meshheading:17493130-Models, Biological,
pubmed-meshheading:17493130-Protein Structure, Quaternary,
pubmed-meshheading:17493130-Protein Structure, Secondary,
pubmed-meshheading:17493130-Protein Transport,
pubmed-meshheading:17493130-Recombinant Fusion Proteins,
pubmed-meshheading:17493130-Spores, Bacterial,
pubmed-meshheading:17493130-Time Factors
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pubmed:year |
2007
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pubmed:articleTitle |
A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis.
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pubmed:affiliation |
Institute for the Biotechnology of Infectious Diseases, University of Technology, Sydney, NSW 2007, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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