Cell division in cocci: localization and properties of the <i>Streptococcus pneumoniae</i> FtsA protein

Lara, Beatríz; Rico, Ana Isabel; Petruzzelli, Sabrina; Santona, Antonella; Dumas, Jacques; Biton, Jacques; Vicente, Miguel; Mingorance, Jesús; Massidda, Orietta

doi:10.1111/j.1365-2958.2004.04432.x

Cited by 117 publications

(149 citation statements)

References 54 publications

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“…These results suggest that the FtsA* plays a role in organizing Z-ring assembly and in the final scission event. These events may involve assembly of FtsA* into polymers on the membrane, which serve to organize FtsZ protofilaments (2,3). Another possibility is that the bond between FtsA* and the Cterminal peptide of FtsZ, which was reported to be very weak, K d ∼ 50 μM (3), may be more readily reversible than the direct insertion of the mts of FtsZ-YFP-mts into the bilayer.…”

Section: Discussionmentioning

confidence: 99%

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Liposome division by a simple bacterial division machinery

Osawa

Erickson

2013

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

192

180

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We previously reconstituted Z rings in tubular multilamellar liposomes with FtsZ-YFP-mts, where mts is a membrane-targeting amphiphilic helix. These reconstituted Z rings generated a constriction force but did not divide the thick-walled liposomes. Here we developed a unique system to observe Z rings in unilamellar liposomes. FtsZ-YFP-mts incorporated inside large, unilamellar liposomes formed patches that produced concave distortions when viewed at the equator of the liposome. When viewed en face at the top of the liposome, many of the patches were seen to be small Z rings, which still maintained the concave depressions. We also succeeded in reconstituting the more natural, two-protein system, with FtsA and FtsZ-YFP (having the FtsA-binding peptide instead of the mts). Unilamellar liposomes incorporating FtsA and FtsZ-YFP showed a variety of distributions, including foci and linear arrays. A small fraction of liposomes had obvious Z rings. These Z rings could constrict the liposomes and in some cases appeared to complete the division, leaving a clear septum between the two daughter liposomes. Because complete liposome divisions were not seen with FtsZ-mts, FtsA may be critical for the final membrane scission event. We demonstrate that reconstituted cell division machinery apparently divides the liposome in vitro.acterial cytokinesis is generated by a complex ring-shaped structure comprising more than a dozen proteins. It is called a Z ring because the primary cytoskeletal framework is made by filamentous temperature-sensitive Z (FtsZ). FtsZ has a globular core homologous to tubulin, and at its C terminus there is an ∼50 amino acid unstructured peptide linker, followed by an ∼17 amino acid peptide that binds FtsA (see ref.

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Section: Discussionmentioning

confidence: 99%

“…FtsA is also the primary dock for most of the downstream division proteins. FtsA proteins from Streptococcus pneumoniae and Thermotoga maritima have been shown to assemble into actin-like filaments in vitro (2,3). FtsA from Escherichia coli has been described as "recalcitrant" and difficult to work with in vitro (4).…”

mentioning

confidence: 99%

Liposome division by a simple bacterial division machinery

Osawa

Erickson

2013

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

192

180

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“…As in the model organisms E. coli and B. subtilis, FtsZ and FtsA are the first proteins to arrive at midcell in S. pneumoniae and form the Zring before cell division initiates (47,48). Once formed, the Zring recruits the later cell-division proteins such as the membrane connectors, DivIVA, and the enzymes required for septal cell-wall synthesis [PBPs, likely PBP2x and PBP1a (4,43)].…”

Section: Discussionmentioning

confidence: 99%

Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP

Beilharz

Novaková

Fadda

et al. 2012

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

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158

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How the human pathogen Streptococcus pneumoniae coordinates cell-wall synthesis during growth and division to achieve its characteristic oval shape is poorly understood. The conserved eukaryotic-type Ser/Thr kinase of S. pneumoniae , StkP, previously was reported to phosphorylate the cell-division protein DivIVA. Consistent with a role in cell division, GFP-StkP and its cognate phosphatase, GFP-PhpP, both localize to the division site. StkP localization depends on its penicillin-binding protein and Ser/Thr-associated domains that likely sense uncross-linked peptidoglycan, because StkP and PhpP delocalize in the presence of antibiotics that target the latest stages of cell-wall biosynthesis and in cells that have stopped dividing. Time-lapse microscopy shows that StkP displays an intermediate timing of recruitment to midcell: StkP arrives shortly after FtsA but before DivIVA. Furthermore, StkP remains at midcell longer than FtsA, until division is complete. Cells mutated for stkP are perturbed in cell-wall synthesis and display elongated morphologies with multiple, often unconstricted, FtsA and DivIVA rings. The data show that StkP plays an important role in regulating cell-wall synthesis and controls correct septum progression and closure. Overall, our results indicate that StkP signals information about the cell-wall status to key cell-division proteins and in this way acts as a regulator of cell division.

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“…The Streptococcus pneumoniae FtsA protein polymerizes in vitro in the presence of ATP (112), and removal of the E. coli membrane-targeting sequence is associated with formation of FtsA filaments within the cytoplasm (159). The ability of cytoplasmic FtsA to form polymeric filaments in vitro and the formation of FtsA filaments in E. coli suggest that FtsA may play a cytoskeleton-like role in the structure of the cytokinetic ring or in the septation process itself, in addition to its role in anchoring FtsZ to the membrane.…”

Section: Tubulin Homologsmentioning

confidence: 99%

The Bacterial Cytoskeleton

Shih

Rothfield

2006

Microbiol Mol Biol Rev

238

220

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SUMMARY In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA group, that appears to be unique to bacteria. The cytoskeletal structures play important roles in cell division, cell polarity, cell shape regulation, plasmid partition, and other functions. The proteins self-assemble into filamentous structures in vitro and form intracellular ordered structures in vivo. In addition, there are a number of filamentous bacterial elements that may turn out to be cytoskeletal in nature. This review attempts to summarize and integrate the in vivo and in vitro aspects of these systems and to evaluate the probable future directions of this active research field.

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Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein

Cited by 117 publications

References 54 publications

Liposome division by a simple bacterial division machinery

Liposome division by a simple bacterial division machinery

Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP

The Bacterial Cytoskeleton

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