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Disassembly of the divisome in E scherichia coli : evidence that FtsZ dissociates before compartmentalization
Author(s) -
Söderström Bill,
Skoog Karl,
Blom Hans,
Weiss David S.,
Heijne Gunnar,
Daley Daniel O.
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12534
Subject(s) - ftsz , cytoplasm , fluorescence recovery after photobleaching , biology , microbiology and biotechnology , compartmentalization (fire protection) , cell division , cell envelope , escherichia coli , cytoskeleton , cytokinesis , cell , biochemistry , membrane , gene , enzyme
Summary 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 E scherichia 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 .