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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1997-2-28
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pubmed:abstractText |
Two new mutations in the cell division gene ftsW have been isolated and characterized. The ftsW263(Ts) mutation results in a block to division at the initiation stage, similar to that previously observed with the ftsW201(Ts) mutation. The ftsW1640(Ts) mutation, however, causes a block to division at a later stage. The ftsW201 and ftsW263 mutants were shown to be phenotypically sensitive to the genetic background and growth conditions and are possibly relA dependent. Immunofluorescence microscopy showed that the FtsZ protein can localize to presumptive division sites in strains carrying ftsW(Ts) mutations at the nonpermissive temperature, suggesting that FtsW is unlikely to be specifically required for the localization of FtsZ to the division site. Examination of the localization of FtsZ in an ftsW rodA double mutant (lemon-shaped cells) revealed several classes of cells ranging from a common class where an FtsZ ring structure is absent to a class where FtsZ forms a complete ring at the midpoint of a lemon-shaped cell, suggesting a role for FtsW in the establishment of a stable FtsZ-based septal structure. We further demonstrate that two FtsW peptides, FtsWL (large) and FtsWS (small), can be identified and that the expression of ftsWS is sufficient for complementation of ftsW(Ts) mutations.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-12736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-1379670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-1528267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-1528268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-1563353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-1944597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-2005134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-2005135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-2509435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-2644207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-2676977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-3009484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-3549457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-363690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-3881765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-3894330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-4577747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-6243629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-6451612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-7569993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-7592387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-7704669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-7815948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-7961485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8169229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8407846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8412689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8412693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8430073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8531889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8552673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8600030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8682793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9006034-8930908
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsW protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/FtsZ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RodA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/guanosine 3',5'-polyphosphate...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
179
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
784-93
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9006034-Alleles,
pubmed-meshheading:9006034-Amino Acid Sequence,
pubmed-meshheading:9006034-Bacterial Proteins,
pubmed-meshheading:9006034-Cell Compartmentation,
pubmed-meshheading:9006034-Cell Division,
pubmed-meshheading:9006034-Cytoskeletal Proteins,
pubmed-meshheading:9006034-Escherichia coli,
pubmed-meshheading:9006034-Escherichia coli Proteins,
pubmed-meshheading:9006034-Fluorescent Antibody Technique,
pubmed-meshheading:9006034-GTP-Binding Proteins,
pubmed-meshheading:9006034-Ligases,
pubmed-meshheading:9006034-Membrane Proteins,
pubmed-meshheading:9006034-Molecular Sequence Data,
pubmed-meshheading:9006034-Mutation,
pubmed-meshheading:9006034-Phenotype,
pubmed-meshheading:9006034-Reading Frames,
pubmed-meshheading:9006034-Sequence Analysis, DNA
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pubmed:year |
1997
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pubmed:articleTitle |
Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function.
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pubmed:affiliation |
Institute of Cell and Molecular Biology, University of Edinburgh, Scotland. mkhattar@srv0.bio.ed.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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