Crystal structure of FtsA from <i>Staphylococcus aureus</i>

Fujita, Junnosuke; Maeda, Y.; Nagao, Chioko; Tsuchiya, Yuko; Miyazaki, Yuma; Hirose, Mika; Mizohata, Eiichi; Matsumoto, Yoshimi; Inoue, Tsuyoshi; Mizuguchi, Kenji; Matsumura, Hideki

doi:10.1016/j.febslet.2014.04.008

Cited by 34 publications

(31 citation statements)

References 34 publications

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“…Together, these data suggest that FtsA plays a role in FtsZ disassembly or turnover (Figure 2B). In support of this idea, purified FtsA from the Gram-positive cocci S. aureus 37 or Deinococcus radiodurans 42 stimulates the GTPase activity of its cognate FtsZ, which would correlate with FtsZ filament disassembly. In contrast, however, D. radiodurans FtsA reduces GTPase activity of E. coli FtsZ.…”

Section: Assembly Of the Proto-ringmentioning

confidence: 94%

“…Several years ago, FtsA from Thermotoga maritima was shown to assemble into actin-like protofilaments that correspond to filaments attached to artificial lipid monolayers 34 . Mutations predicted to disrupt subunit interactions and subsequent formation of these filaments 35 were tested in B. subtilis and found to lead to defects in cell division, suggesting that the degree of FtsA oligomerization or polymerization was important for integrity of the proto-ring 36 Interestingly, a recent crystal structure of S. aureus FtsA reveals FtsA oligomers with a 28° inter-subunit twist relative to the T. maritima protein 37 . Although this topology has not yet been confirmed on membranes, the evidence underscores the potential species-specific conformational diversity of FtsA, which may complicate generalizations based on a single crystal structure.…”

Section: Assembly Of the Proto-ringmentioning

confidence: 99%

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Splitsville: structural and functional insights into the dynamic bacterial Z ring

Haeusser

Margolin²

2016

Nat Rev Microbiol

299

283

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Preface Bacteria must divide in order to increase in number and colonize their niche. Binary fission is the most widespread means of bacterial cell division, but even this relatively simple mechanism displays many variations on a theme. In most bacteria, the tubulin homolog FtsZ assembles into a ring structure (Z ring) at the site of cytokinesis and recruits additional proteins to form a large protein machine (divisome) that spans the membrane. Here we discuss current insights into the regulation of Z ring assembly and how the divisome drives membrane invagination and septal cell wall growth while still flexibly responding to various cellular inputs.

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Section: Assembly Of the Proto-ringmentioning

confidence: 94%

Section: Assembly Of the Proto-ringmentioning

confidence: 99%

Splitsville: structural and functional insights into the dynamic bacterial Z ring

Haeusser

Margolin²

2016

Nat Rev Microbiol

299

283

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“…To determine how individual FtsA monomers might interact in such a structure, we docked the published FtsA atomic structure from Staphylococcus aureus 4748, into the densities. The docking model fitted 12 subunits into the miniring structure as a hexamer of dimers (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The class average of hexagonally packed rings without a filament density was used for the fitting of the crystal structure of S. aureus FtsA in complex with ATP (PDB: 3WQU)48 using UCSF Chimera80. The A and B chains of one copy were manually fit into the density and we optimized its placement by localized rigid-body fitting.…”

Section: Methodsmentioning

confidence: 99%

Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments

Krupka¹,

Rowlett

Morado³

et al. 2017

Nat Commun

117

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Most bacteria divide using a protein machine called the divisome that spans the cytoplasmic membrane. Key divisome proteins on the membrane’s cytoplasmic side include tubulin-like FtsZ, which forms GTP-dependent protofilaments, and actin-like FtsA, which tethers FtsZ to the membrane. Here we present genetic evidence that in Escherichia coli, FtsA antagonizes FtsZ protofilament bundling in vivo. We then show that purified FtsA does not form straight polymers on lipid monolayers as expected, but instead assembles into dodecameric minirings, often in hexameric arrays. When coassembled with FtsZ on lipid monolayers, these FtsA minirings appear to guide FtsZ to form long, often parallel, but unbundled protofilaments, whereas a mutant of FtsZ (FtsZ*) with stronger lateral interactions remains bundled. In contrast, a hypermorphic mutant of FtsA (FtsA*) forms mainly arcs instead of minirings and enhances lateral interactions between FtsZ protofilaments. Based on these results, we propose that FtsA antagonizes lateral interactions between FtsZ protofilaments, and that the oligomeric state of FtsA may influence FtsZ higher-order structure and divisome function.

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“…The ftsA gene sequences have not been used in the phylogenetic analysis of root nodule bacteria. The FtsA protein functions at the earliest stage of bacterial division, connecting FtsZ, the principal component of the division machinery, to the cell membrane, and forms a structure called the proto-ring at the division site (Fujita et al 2014). FtsA belongs structurally to the actin/Hsp70/hexokinase superfamily and is widespread in bacteria (Busiek and Margolin 2015).…”

Section: Introductionmentioning

confidence: 99%

The ftsA gene as a molecular marker for phylogenetic studies in Bradyrhizobium and identification of Bradyrhizobium japonicum

Kalita

Małek

2018

J Appl Genetics

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The use of ftsA gene sequences for taxonomic studies of the genus Bradyrhizobium bacteria was assessed. The ftsA gene codes for an actin-like protein involved in prokaryotic cell division. Up to now, this gene has not been used as a phylogenetic marker for analysis of bacteria establishing root nodule symbiosis with Fabaceae plants. In this study, the ftsA gene sequences obtained for bradyrhizobia forming N 2 fixing symbiosis with four Genisteae tribe plants growing in Poland and most of the type strains of the genus Bradyrhizobium species were analyzed and evaluated as molecular markers for phylogenetic studies of these bacteria for the first time. The ftsA gene sequences of all bradyrhizobial strains with completely or partially sequenced genomes, available in the GenBank database, were also included into the analysis. The phylogeny of the ftsA gene was compared to the phylogenies of other chromosomal genes commonly used in the studies of Bradyrhizobium bacteria. The results showed that the phylogenies of ftsA and the core genes recA and glnII were congruent, making the ftsA gene useful as a phylogenetic marker. Analysis of the ftsA gene sequences revealed a single-nucleotide polymorphism unique to Bradyrhizobium japonicum strains, and the potential use of this SNP for identification of this species was discussed. Electronic supplementary material The online version of this article (10.1007/s13353-018-0479-9) contains supplementary material, which is available to authorized users.

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Crystal structure of FtsA from Staphylococcus aureus

Cited by 34 publications

References 34 publications

Splitsville: structural and functional insights into the dynamic bacterial Z ring

Splitsville: structural and functional insights into the dynamic bacterial Z ring

Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments

The ftsA gene as a molecular marker for phylogenetic studies in Bradyrhizobium and identification of Bradyrhizobium japonicum

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