FtsZ Polymer-bundling by the Escherichia coli ZapA Orthologue, YgfE, Involves a Conformational Change in Bound GTP

Small, Elaine; Marrington, Rachel; Rodger, Alison; Scott, David J.; Sloan, Katherine E.; Roper, David I.; Dafforn, Timothy R.; Addinall, Stephen G.

doi:10.1016/j.jmb.2007.03.025

Cited by 87 publications

(138 citation statements)

References 50 publications

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“…ZapA binds to FtsZ to promote Z-ring assembly (10,68) and has been used as a marker for FtsZ localization and dynamics (69,70). iPALM images of mEos2-ZapA in BW25113 cells showed punctate structures similar to those of FtsZ-mEos2 (SI Appendix, Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Once established, the Z-ring recruits an ensemble of transmembrane and periplasmic proteins involved in cell wall peptidoglycan (PG) synthesis and remodeling, including the essential transpeptidase and penicillinbinding protein PBP3 (also called FtsI) (8,9). Recently, a new group of Z-ring-associated proteins (Zaps) has been shown to stabilize the Z-ring (10)(11)(12)(13)(14)(15). Some of these Zaps connect the Z-ring to the bacterial chromosome through a multilayered protein network that includes the chromosome-binding protein MatP (16)(17)(18)(19).…”

mentioning

confidence: 99%

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Defining the rate-limiting processes of bacterial cytokinesis

Coltharp

Buss

Plumer

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

161

216

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Bacterial cytokinesis is accomplished by the essential ‘divisome’ machinery. The most widely conserved divisome component, FtsZ, is a tubulin homolog that polymerizes into the ‘FtsZ-ring’ (‘Z-ring’). Previous in vitro studies suggest that Z-ring contraction serves as a major constrictive force generator to limit the progression of cytokinesis. Here, we applied quantitative superresolution imaging to examine whether and how Z-ring contraction limits the rate of septum closure during cytokinesis in Escherichia coli cells. Surprisingly, septum closure rate was robust to substantial changes in all Z-ring properties proposed to be coupled to force generation: FtsZ’s GTPase activity, Z-ring density, and the timing of Z-ring assembly and disassembly. Instead, the rate was limited by the activity of an essential cell wall synthesis enzyme and further modulated by a physical divisome–chromosome coupling. These results challenge a Z-ring–centric view of bacterial cytokinesis and identify cell wall synthesis and chromosome segregation as limiting processes of cytokinesis.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Defining the rate-limiting processes of bacterial cytokinesis

Coltharp

Buss

Plumer

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

161

216

View full text Add to dashboard Cite

show abstract

“…One of the first discovered was ZipA, which bundles most efficiently at a pH of Ͻ6 (67,156). ZapA, a protein that enhances Z-ring stability, generates a variety of bundled forms (65,101,119,178). ZapB, a small coiled-coil protein that stimulates Z-ring assembly, induces FtsZ bundles with a striking ϳ10-nm banding pattern.…”

Section: Lateral Bonds: Do They Exist?mentioning

confidence: 99%

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Erickson

Anderson

Osawa

2010

Microbiol Mol Biol Rev

558

752

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SUMMARY FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside tubular liposomes. Moreover, these artificial Z rings can generate a constriction force, demonstrating that FtsZ is its own force generator. Here we review light microscope observations of how Z rings assemble in bacteria. Assembly begins with long-pitch helices that condense into the Z ring. Once formed, the Z ring can transition to short-pitch helices that are suggestive of its structure. FtsZ assembles in vitro into short protofilaments that are ∼30 subunits long. We present models for how these protofilaments might be further assembled into the Z ring. We discuss recent experiments on assembly dynamics of FtsZ in vitro, with particular attention to how two regulatory proteins, SulA and MinC, inhibit assembly. Recent efforts to develop antibacterial drugs that target FtsZ are reviewed. Finally, we discuss evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation.

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“…The FtsZ filament pelleting assay was carried out on as described previously (Small et al 2007) except that the initial volume was 100 mL. Samples contained FtsZ Tfus together with either SsgB Tfus or (as negative control) BSA.…”

Section: In Vitro Polymerization Of Ftsz and Pelleting Assaymentioning

confidence: 99%

Positive control of cell division: FtsZ is recruited by SsgB during sporulation ofStreptomyces

Willemse¹,

Borst²,

Waal³

et al. 2011

Genes Dev.

171

201

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In bacteria that divide by binary fission, cell division starts with the polymerization of the tubulin homolog FtsZ at mid-cell to form a cell division scaffold (the Z ring), followed by recruitment of the other divisome components. The current view of bacterial cell division control starts from the principle of negative checkpoints that prevent incorrect Z-ring positioning. Here we provide evidence of positive control of cell division during sporulation of Streptomyces, via the direct recruitment of FtsZ by the membrane-associated divisome component SsgB. In vitro studies demonstrated that SsgB promotes the polymerization of FtsZ. The interactions are shown in vivo by time-lapse imaging and Fö rster resonance energy transfer and fluorescence lifetime imaging microscopy (FRET-FLIM), and are corroborated independently via two-hybrid studies. As determined by fluorescence recovery after photobleaching (FRAP), the turnover of FtsZ protofilaments increased strongly at the time of Z-ring formation. The surprising positive control of Z-ring formation by SsgB implies the evolution of an entirely new way of Z-ring control, which may be explained by the absence of a mid-cell reference point in the long multinucleoid hyphae. In turn, the localization of SsgB is mediated through the orthologous SsgA, and premature expression of the latter is sufficient to directly activate multiple Z-ring formation and hyperdivision at early stages of the Streptomyces cell cycle.

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FtsZ Polymer-bundling by the Escherichia coli ZapA Orthologue, YgfE, Involves a Conformational Change in Bound GTP

Cited by 87 publications

References 50 publications

Defining the rate-limiting processes of bacterial cytokinesis

Defining the rate-limiting processes of bacterial cytokinesis

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Positive control of cell division: FtsZ is recruited by SsgB during sporulation ofStreptomyces

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