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- W1983767270 abstract "E. coli cell division is achieved by the concerted effort of at least 13 essential proteins that assemble at midcell in a cell-cycle dependent manner to form a macromolecular structure (divisome) capable of generating septal force. Central to divisome assembly is the initial formation of the Z-ring, a dynamic, cytokinetic suprastructure of the FtsZ protein, the prokaryotic tubulin homolog widely conserved in bacteria. Being the first division protein to localize precisely to midcell, spatial and temporal regulation of FtsZ polymerization is of critical importance to efficient proliferation. From conventional fluorescence microscopy, the Z-ring has long been regarded as a closed-ring that circumscribes the cell. However, in vitro studies illustrated FtsZ's tendency to self-assemble into short, single-stranded protofilaments that further coalesce into multi-stranded rings and helices under molecular crowding conditions. Recently, our group has shown that the relevant in vivo structure of FtsZ is characterized by an irregular, discontinuous arrangement of overlapping protofilaments, observed in a closed ring as well as a compressed helical conformation. We believe that an equilibrium exists between the helix and ring conformations and therefore factors promoting the transition from helix to ring may serve as critical regulatory elements or pathways. ZapA and ZapB are both non-essential, cytoplasmic proteins that associate directly with FtsZ early during division. Although their null mutants have little observable cytokinetic defect, both have a pronounced prevalence of FtsZ helical conformations, indicating their presence favors ring formation. In this study, we employ super-resolution imaging to characterize the relevant in vivo arrangements of ZapA and ZapB, as well as their relative localization with respect to FtsZ using two-color imaging methods. Lastly, by characterizing the helical conformation the Z-ring in the Zap-null mutants, we gain insight to their potential regulatory mechanism." @default.
- W1983767270 created "2016-06-24" @default.
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- W1983767270 date "2012-01-01" @default.
- W1983767270 modified "2023-09-26" @default.
- W1983767270 title "Regulating Bacterial Cytokinesis: A Super-Resolution Study of ZapA and ZapB" @default.
- W1983767270 doi "https://doi.org/10.1016/j.bpj.2011.11.2105" @default.
- W1983767270 hasPublicationYear "2012" @default.
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