Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli
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چکیده
منابع مشابه
Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli.
The bacterial cell division protein FtsZ assembles into the cytokinetic Z ring that directs cytokinesis in prokaryotes. In Escherichia coli the formation of the Z ring is prevented by induction of the cell division inhibitor SulA (SfiA), a component of the SOS response. Here we show that a MalE-SulA fusion that retains this inhibitory function in vivo inhibits the GTPase activity and polymeriza...
متن کاملInvestigation of regulation of FtsZ assembly by SulA and development of a model for FtsZ polymerization.
In Escherichia coli FtsZ organizes into a cytoskeletal ring structure, the Z ring, which effects cell division. FtsZ is a GTPase, but the free energy of GTP hydrolysis does not appear to be used for generation of the constriction force, leaving open the question of the function of the GTPase activity of FtsZ. Here we study the mechanism by which SulA, an inhibitor of FtsZ induced during the SOS...
متن کاملRole of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells.
Induction of the SOS response in Escherichia coli by DNA-damaging treatments results in the synthesis of the SulA polypeptide, and this is sufficient to cause the resulting inhibition of cell division. Mutations at either sulA (sfiA) or sulB (sfiB) suppress this division inhibition. The SulB protein is identical to FtsZ, a protein required for normal division in E. coli. In the presence of FtsZ...
متن کاملA point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase.
The cell division protein FtsZ, essential to initiate septum formation in Escherichia coli, is a GTPase. The thermosensitive ftsZ84 mutation, which impairs the ability of FtsZ to bind and hydrolyze GTP in vitro, maps to a short glycine-rich FtsZ segment. This region is conserved in eubacterial FtsZ homologs and is strikingly similar to the proposed GTP binding motif in the eukaryotic cytoskelet...
متن کاملSulA inhibits assembly of FtsZ by a simple sequestration mechanism.
We have investigated the inhibition by SulA of the assembly of Escherichia coli FtsZ. Using quantitative GTPase and fluorescence assays, we found that SulA inhibition resulted in an increase in the apparent critical concentration for FtsZ assembly. The increase in apparent critical concentration was always less than the total amount of SulA added, suggesting that the association of SulA and Fts...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.6.2885