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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 |
1998-7-24
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pubmed:abstractText |
Using immunofluorescence microscopy, we have found that SeqA protein, a regulator of replication initiation, is localized as discrete fluorescent foci in E. coli wild-type cells. Surprisingly, SeqA foci were observed also in an oriC deletion mutant. Statistical analysis revealed that a SeqA focus is localized at midcell in newborn cells. The SeqA focus is duplicated and tethered at midcell until an FtsZ ring is formed. Subsequently, these foci migrate in opposite directions toward cell quarter sites and remain tethered there until the cell divides. The cell cycle-dependent bidirectional migration of SeqA-DNA complexes is quite different from the migration pattern of oriC Dna copies. MukB protein is required for correct localization of SeqA complexes by an unknown mechanism.
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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 Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding 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/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MukB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SeqA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
381-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9660922-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9660922-Bacterial Proteins,
pubmed-meshheading:9660922-Cell Division,
pubmed-meshheading:9660922-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9660922-Chromosomes, Bacterial,
pubmed-meshheading:9660922-Culture Media,
pubmed-meshheading:9660922-Cytoskeletal Proteins,
pubmed-meshheading:9660922-DNA, Bacterial,
pubmed-meshheading:9660922-DNA Replication,
pubmed-meshheading:9660922-DNA-Binding Proteins,
pubmed-meshheading:9660922-Escherichia coli,
pubmed-meshheading:9660922-Escherichia coli Proteins,
pubmed-meshheading:9660922-GTP-Binding Proteins,
pubmed-meshheading:9660922-Gene Deletion,
pubmed-meshheading:9660922-In Situ Hybridization, Fluorescence,
pubmed-meshheading:9660922-Mutagenesis,
pubmed-meshheading:9660922-RNA, Messenger,
pubmed-meshheading:9660922-Replication Origin,
pubmed-meshheading:9660922-Transcription Factors
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pubmed:year |
1998
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pubmed:articleTitle |
Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli.
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pubmed:affiliation |
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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