SlmA Antagonism of FtsZ Assembly Employs a Two-pronged Mechanism like MinCD

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Bacteria divide in the middle of the cell by spatially regulating the position of the Z ring, a cytoskeletal element required for cytokinesis. In the model organisms, Escherichia coli and Bacillus subtilis, two negative regulatory systems contribute to this spatial regulation. Both systems contain antagonists of FtsZ assembly that are localized in the cell. In this study we isolated FtsZ mutants resistant to SlmA, which is positioned within the cell by binding to sites asymmetrically distributed around the chromosome. We confirm that SlmA is activated by DNA binding to antagonize FtsZ polymerization in vitro and that the newly isolated mutants are resistant. We also show that SlmA binds to the very conserved tail of FtsZ and that this is required to antagonize FtsZ assembly even though the tail is not required for polymerization. Together, these results highlight the importance of the tail of FtsZ and lead to a model in which SlmA binding to the tail of FtsZ results in further interactions that break the filament. This mechanism is shared with the other spatial regulator and raises the possibility that it may be a common mechanism among spatial regulators of Z ring assembly.

Vyšlo v časopise: SlmA Antagonism of FtsZ Assembly Employs a Two-pronged Mechanism like MinCD. PLoS Genet 10(7): e32767. doi:10.1371/journal.pgen.1004460
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004460

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