Super-resolution imaging of the bacterial cytokinetic protein FtsZ

Jennings, Phoebe C.; Cox, Guy; Monahan, Leigh G.; Harry, Elizabeth J.

doi:10.1016/j.micron.2010.09.003

Cited by 56 publications

(56 citation statements)

References 38 publications

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“…The precise organization of FtsZ filaments in the Z ring has not been resolved. However, recent cryo-electron microscopy (EM) tomography and superresolution imaging data suggest that lateral contacts between FtsZ molecules in the Z ring are loosely arranged (6)(7)(8)(9). Notably, the intracellular levels of FtsZ remain unchanged during the cell cycle and exceed the critical concentration required for Z-ring formation (3).…”

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confidence: 99%

SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid

Tonthat¹,

Milam

Chinnam³

et al. 2013

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

107

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The authors note that on page 13064, right column, first full paragraph, lines 4-7, "Some of the climatic events linked to such concerns are the severe droughts experienced by the Amazon basin in 2005 and 2010, which reportedly reduced tropical forest NPP by 1.6 to 2.2 PgC/y and increased tree mortality (50, 51)" should instead appear as "Some of the climatic events linked to such concerns are the severe droughts experienced by the Amazon basin in 2005 and 2010, which reportedly reduced tropical forest NPP and increased tree mortality by a total biomass carbon loss of 1.6 to 2.2 PgC (50, 51)."On page 13064, right column, first full paragraph, lines 12-17, "Assuming that the large reductions of tropical NPP reported previously (50, 51) are realistic, the absence of marked variations of the global CO 2 growth rate after the 2005 and 2010 Amazon droughts may imply that the drought conditions also coincidently reduced tropical Rh along with NPP, resulting in (relatively) small NEE anomalies" should instead appear as "Assuming that the large reductions of tropical forest biomass reported previously (50, 51) are realistic, the absence of marked variations of the global CO 2 growth rate after the 2005 and 2010 Amazon droughts may imply that the drought conditions also coincidently reduced tropical Rh along with NPP, resulting in (relatively) small NEE anomalies."These changes do not affect the conclusions of the article.

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mentioning

confidence: 99%

SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid

Tonthat¹,

Milam

Chinnam³

et al. 2013

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

107

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“…Using similar techniques, Shih et al then reported that MreB (and three other proteins) formed extended helices in Escherichia coli as well (27). Numerous publications have since claimed that MreB and various other proteins polymerize into extended helices that encircle diverse rod-shaped bacteria (5,8,15,22,30,31,36). Data supporting these claims include fluorescence microscopy of both cells harboring fluorescent protein fusions and wild-type cells probed with fluorescently labeled antibodies.…”

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confidence: 97%

The Helical MreB Cytoskeleton in Escherichia coli MC1000/pLE7 Is an Artifact of the N-Terminal Yellow Fluorescent Protein Tag

2012

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Based on fluorescence microscopy, the actin homolog MreB has been thought to form extended helices surrounding the cytoplasm of rod-shaped bacterial cells. The presence of these and other putative helices has come to dominate models of bacterial cell shape regulation, chromosome segregation, polarity, and motility. Here we use electron cryotomography to show that MreB does in fact form extended helices and filaments in Escherichia coli when yellow fluorescent protein (YFP) is fused to its N terminus but native (untagged) MreB expressed to the same levels does not. In contrast, mCherry fused to an internal loop (MreB-RFP SW ) does not induce helices. The helices are therefore an artifact of the placement of the fluorescent protein tag. YFP-MreB helices were also clearly distinguishable from the punctate, "patchy" localization patterns of MreB-RFP SW , even by standard light microscopy. The many interpretations in the literature of such punctate patterns as helices should therefore be reconsidered.

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“…S1A) (6)(7)(8)(9). FtsZ self-assembles into linear protofilaments in a GTP-dependent manner by interactions between its globular domains, and data suggest that loosely arranged lateral contacts between protofilaments mediate the formation of the Z ring at the cell center (10)(11)(12)(13)(14)(15)(16). Notably, the intracellular levels of FtsZ remain largely unchanged during the cell cycle and exceed the critical concentration required for Z-ring formation (17).…”

mentioning

confidence: 99%

Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ

Schumacher

Zhang

2016

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

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Cell division in most prokaryotes is mediated by FtsZ, which polymerizes to create the cytokinetic Z ring. Multiple FtsZ-binding proteins regulate FtsZ polymerization to ensure the proper spatiotemporal formation of the Z ring at the division site. The DNA-binding protein SlmA binds to FtsZ and prevents Z-ring formation through the nucleoid in a process called "nucleoid occlusion" (NO). As do most FtsZ-accessory proteins, SlmA interacts with the conserved C-terminal domain (CTD) that is connected to the FtsZ core by a long, flexible linker. However, SlmA is distinct from other regulatory factors in that it must be DNA-bound to interact with the FtsZ CTD. Few structures of FtsZ regulator-CTD complexes are available, but all reveal the CTD bound as a helix. To deduce the molecular basis for the unique SlmA-DNA-FtsZ CTD regulatory interaction and provide insight into FtsZ-regulator protein complex formation, we determined structures of Escherichia coli, Vibrio cholera, and Klebsiella pneumonia SlmA-DNA-FtsZ CTD ternary complexes. Strikingly, the FtsZ CTD does not interact with SlmA as a helix but binds as an extended conformation in a narrow, surface-exposed pocket formed only in the DNA-bound state of SlmA and located at the junction between the DNA-binding and C-terminal dimer domains. Binding studies are consistent with the structure and underscore key interactions in complex formation. Combined, these data reveal the molecular basis for the SlmA-DNA-FtsZ interaction with implications for SlmA's NO function and underscore the ability of the FtsZ CTD to adopt a wide range of conformations, explaining its ability to bind diverse regulatory proteins.n Escherichia coli cell division is directed by a cytoskeletal element called the "Z ring," which is formed at the cell membrane by the tubulin-like protein, FtsZ (1-5). FtsZ is an ancient and highly conserved protein that mediates cell division in most bacteria, many archaea, chloroplasts, and the mitochondria of primitive eukaryotes (5). FtsZ consists of three main domains: a globular core that harbors the GTP-binding site, a flexible C-terminal linker (CTL) that is ∼50 residues long in E. coli but is of variable length among FtsZ homologs, and a C-terminal domain (CTD) comprised of a highly conserved set of residues followed by a short and less conserved, variable (CTV) region (Fig. S1A) (6-9). FtsZ self-assembles into linear protofilaments in a GTP-dependent manner by interactions between its globular domains, and data suggest that loosely arranged lateral contacts between protofilaments mediate the formation of the Z ring at the cell center (10-16). Notably, the intracellular levels of FtsZ remain largely unchanged during the cell cycle and exceed the critical concentration required for Z-ring formation (17). A diverse repertoire of FtsZ-binding regulatory proteins has evolved that affect FtsZ localization and polymerization to ensure that the Z ring is created at the correct place and time during cell division (2)(3)(4)(18)(19)(20). In the model bacteria E. coli a...

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Super-resolution imaging of the bacterial cytokinetic protein FtsZ

Cited by 56 publications

References 38 publications

SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid

SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid

The Helical MreB Cytoskeleton in Escherichia coli MC1000/pLE7 Is an Artifact of the N-Terminal Yellow Fluorescent Protein Tag

Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ

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