@article {46531,
	title = {A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.},
	journal = {PLoS Genetics},
	volume = {11},
	year = {2015},
	month = {2015 Apr 07},
	pages = {e1005128},
	abstract = {<p>The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. The FtsZ-ring establishes the division plane and enables the assembly of the macromolecular division machinery (divisome). Although many molecular components of the divisome have been identified and their interactions extensively characterized, the spatial organization of these proteins within the divisome is unclear. Consequently, the physical mechanisms that drive divisome assembly, maintenance, and constriction remain elusive. Here we applied single-molecule based superresolution imaging, combined with genetic and biophysical investigations, to reveal the spatial organization of cellular structures formed by four important divisome proteins in E. coli: FtsZ, ZapA, ZapB and MatP. We show that these interacting proteins are arranged into a multi-layered protein network extending from the cell membrane to the chromosome, each with unique structural and dynamic properties. Further, we find that this protein network stabilizes the FtsZ-ring, and unexpectedly, slows down cell constriction, suggesting a new, unrecognized role for this network in bacterial cell division. Our results provide new insight into the structure and function of the divisome, and highlight the importance of coordinated cell constriction and chromosome segregation.</p>
},
	issn = {1553-7404},
	doi = {10.1371/journal.pgen.1005128},
	author = {Buss, Jackson and Coltharp, Carla and Shtengel, Gleb and Yang, Xinxing and Hess, Harald and Xiao, Jie}
}
