Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization
2014 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 92, no 1, 1-9 p.Article in journal (Refereed) Published
In most bacteria cell division is mediated by a protein super-complex called the divisome that co-ordinates the constriction and scission of the cell envelope. FtsZ is the first of the divisome proteins to accumulate at the division site and is widely thought to function as a force generator that constricts the cell envelope. In this study we have used a combination of confocal fluorescence microscopy and fluorescence recovery after photobleaching (FRAP) to determine if divisome proteins are present at the septum at the time of cytoplasmic compartmentalization in Escherichia coli. Our data suggest that many are, but that FtsZ and ZapA disassemble before the cytoplasm is sealed by constriction of the inner membrane. This observation implies that FtsZ cannot be a force generator during the final stage(s) of envelope constriction in E.coli.
Place, publisher, year, edition, pages
2014. Vol. 92, no 1, 1-9 p.
Green Fluorescent Protein, Cell-Division Protein, Z-Ring, Septal Ring, Chromosome Segregation, Bacterial Cytokinesis, Localization, Membrane, Colocalization, Hydrolysis
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-145600DOI: 10.1111/mmi.12534ISI: 000334331300001ScopusID: 2-s2.0-84897109056OAI: oai:DiVA.org:kth-145600DiVA: diva2:723591
FunderSwedish Foundation for Strategic Research EU, European Research Council, ERC-2008-AdG 232648Swedish Research CouncilScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
QC 201406112014-06-112014-05-232014-06-11Bibliographically approved