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Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
Open accessAbstract
The tubulin-like FtsZ protein initiates assembly of the bacterial cytokinetic machinery by polymerizing into a ring structure, the Z ring, at the prospective site of division. To block Z-ring formation over the nucleoid and help coordinate cell division with chromosome segregation, Escherichia coli employs the nucleoid-associated division inhibitor, SlmA. Here, we investigate the mechanism by which SlmA regulates FtsZ assembly. We show that SlmA disassembles FtsZ polymers in vitro. In addition, using chromatin immunoprecipitation (ChIP), we identified 24 SlmA-binding sequences (SBSs) on the chromosome. Remarkably, SlmA binding to SBSs dramatically enhanced its ability to interfere with FtsZ polymerization, and ChIP studies indicate that SlmA regulates FtsZ assembly at these sites in vivo. Because of the dynamic and highly organized nature of the chromosome, coupling SlmA activation to specific DNA binding provides a mechanism for the precise spatiotemporal control of its anti-FtsZ activity within the cell.
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Citations
Cites
Murein segregation in Escherichia coli
de Pedro, M. A., Quintela, J. C., Höltje, J. V., & Schwarz, H. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.9.2823-2834.1997 · Cited by 388
Cited by
Type VI secretion requires a dynamic contractile phage tail-like structure
Basler, M., Pilhofer, M., Henderson, G. P., Jensen, G. J., & Mekalanos, J. J. (2012) · Nature · doi:10.1038/nature10846 · Cited by 673
Cuthbertson, L., & Nodwell, J. R. (2013) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00018-13 · Cited by 554
The physiology of bacterial cell division
Egan, A. J. F., & Vollmer, W. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06818.x · Cited by 320
Bacterial cytokinesis: From Z ring to divisome
Lutkenhaus, J., Pichoff, S., & Du, S. (2012) · Cytoskeleton · doi:10.1002/cm.21054 · Cited by 260
Chien, A.-C., Hill, N. S., & Levin, P. A. (2012) · Current Biology · doi:10.1016/j.cub.2012.02.032 · Cited by 256
Metadata
- Authors
- Cho, H., McManus, H. R., Dove, S. L., & Bernhardt, T. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-02-14
- Volume
- 108
- Issue
- 9
- Pages
- 3773-3778
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2163039084
- Cited by
- 226
- References
- 1
- FWCI
- 14.25
- Type
- journal article
- Language
- en
- Open access
- green
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- Cho, H., McManus, H. R., Dove, S. L., & Bernhardt, T. G. (2011). Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1018674108
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