Prokaryotic cytoskeletons: protein filaments organizing small cells

Wagstaff, Jane L.; Löwe, Jan

doi:10.1038/nrmicro.2017.153

Cited by 109 publications

(119 citation statements)

References 183 publications

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“…In these organisms, cell shape and spatial regulation of peptidoglycan synthesis are both tied to the actin homolog MreB (Dominguez-Escobar et al, 2011;Errington 2015;Gitai et al, 2004;Garner et al, 2011;van den Ent, Amos, van Teeffelen et al, 2011). MreB is one of several bacterial proteins that are now widely accepted as components of the bacterial cytoskeleton, which have been reviewed in (Cabeen & Jacobs-Wagner 2010;Carballido-Lopez & Errington 2003;Errington 2015;Eun et al, 2015;Wagstaff & Lowe 2018). MreB is one of several bacterial proteins that are now widely accepted as components of the bacterial cytoskeleton, which have been reviewed in (Cabeen & Jacobs-Wagner 2010;Carballido-Lopez & Errington 2003;Errington 2015;Eun et al, 2015;Wagstaff & Lowe 2018).…”

Section: Introductionmentioning

confidence: 99%

“…Similar to their eukaryotic homologs, polymerization of bacterial cytoskeletal proteins is important for their roles in cellular functions, including shape maintenance (Carballido-Lopez & Errington 2003;Eun et al, 2015;Wagstaff & Lowe 2018). These proteins also exhibit structural, although not necessarily sequence similarity, to eukaryotic cytoskeleton proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Inhibition of MreB causes the bacteria to transform into spherical (Doi et al, 1988;Gitai et al, 2004;Jones et al, 2001;Wachi et al, 1989) or lemon-shaped cells (Takacs et al, 2010), that for E. coli have been shown to have active peptidoglycan metabolism (Billings et al, 2014;Margolin 2009;Ranjit et al, 2017). MreB is one of several bacterial proteins that are now widely accepted as components of the bacterial cytoskeleton, which have been reviewed in (Cabeen & Jacobs-Wagner 2010;Carballido-Lopez & Errington 2003;Errington 2015;Eun et al, 2015;Wagstaff & Lowe 2018).…”

Section: Introductionmentioning

confidence: 99%

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DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth

et al. 2018

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In many model organisms, diffuse patterning of cell wall peptidoglycan synthesis by the actin homolog MreB enables the bacteria to maintain their characteristic rod shape. In Caulobacter crescentus and Escherichia coli, MreB is also required to sculpt this morphology de novo. Mycobacteria are rod-shaped but expand their cell wall from discrete polar or subpolar zones. In this genus, the tropomyosin-like protein DivIVA is required for the maintenance of cell morphology. DivIVA has also been proposed to direct peptidoglycan synthesis to the tips of the mycobacterial cell. The precise nature of this regulation is unclear, as is its role in creating rod shape from scratch. We find that DivIVA localizes nascent cell wall and covalently associated mycomembrane but is dispensable for the assembly process itself. Mycobacterium smegmatis rendered spherical by peptidoglycan digestion or by DivIVA depletion are able to regain rod shape at the population level in the presence of DivIVA. At the single cell level, there is a close spatiotemporal correlation between DivIVA foci, rod extrusion and concentrated cell wall synthesis. Thus, although the precise mechanistic details differ from other organisms, M. smegmatis also establish and propagate rod shape by cytoskeleton-controlled patterning of peptidoglycan. Our data further support the emerging notion that morphology is a hardwired trait of bacterial cells.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth

et al. 2018

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“…In Escherichia coli, cell division is executed by a large multi-protein complex known as the divisome. The most well conserved component of the divisome is FtsZ, a prokaryotic homolog of tubulin (Erickson et al, 2010;Wagstaff and Löwe, 2018). Cytoplasmic FtsZ is tethered to the inner membrane by two proteins, the actin homolog FtsA and the transmembrane division protein ZipA (Pichoff and Lutkenhaus, 2002), forming an early divisome structure called the proto-ring.…”

Section: Introductionmentioning

confidence: 99%

Gain‐of‐function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling

Schoenemann¹,

Krupka²,

Rowlett³

et al. 2018

Molecular Microbiology

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Escherichia coli requires FtsZ, FtsA and ZipA proteins for early stages of cell division, the latter two tethering FtsZ polymers to the cytoplasmic membrane. Hypermorphic mutants of FtsA such as FtsA* (R286W) map to the FtsA self-interaction interface and can bypass the need for ZipA. Purified FtsA forms closed minirings on lipid monolayers that antagonize bundling of FtsZ protofilaments, whereas FtsA* forms smaller oligomeric arcs that enable bundling. Here, we examined three additional FtsA*-like mutant proteins for their ability to form oligomers on lipid monolayers and bundle FtsZ. Surprisingly, all three formed distinct structures ranging from mostly arcs (T249M), a mixture of minirings, arcs and straight filaments (Y139D) or short straight double filaments (G50E). All three could form filament sheets at higher concentrations with added ATP. Despite forming these diverse structures, all three mutant proteins acted like FtsA* to enable FtsZ protofilament bundling on lipid monolayers. Synthesis of the FtsA*-like proteins in vivo suppressed the toxic effects of a bundling-defective FtsZ, exacerbated effects of a hyper-bundled FtsZ, and rescued some thermosensitive cell division alleles. Together, the data suggest that conversion of FtsA minirings into any type of non-miniring oligomer can promote progression of cytokinesis through FtsZ bundling and other mechanisms.

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“…Our resultsestablish SAXS as areliable structural analysism ethod for long DNA nanotubes and could assist in the rational design of these structures.Genetically encoded nanotubes made from biomacromolecules, such as cytoskeletal filaments, [1] channeling protein nanotubes, [2] and membrane channels, [3] are critical cellular components. However,l ittle is knowna bout the structures of assembled DNA nanotubes in solution.H ere we report an in situ exploration of segmented DNA nanotubes, composed of multiple units with set length distributions, by using synchrotron small-angle X-ray scattering (SAXS).…”

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confidence: 99%

In‐Situ Configuration Studies on Segmented DNA Origami Nanotubes

et al. 2019

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One-dimensional nanotubes are of considerable interest in materials and biochemical sciences.Aparticular desire is to create DNA nanotubes with user-defined structural features and biological relevance, which will facilitate the application of these nanotubes in the controlled release of drugs,t emplating of other materials into linear arrays and the construction of artificial membrane channels. However,l ittle is knowna bout the structures of assembled DNA nanotubes in solution.H ere we report an in situ exploration of segmented DNA nanotubes, composed of multiple units with set length distributions, by using synchrotron small-angle X-ray scattering (SAXS). Through joint experimental and theoretical studies, we show that the SAXS data are highly informativei nt he context of heterogeneous mixtures of DNA nanotubes. The structural parameters obtained by SAXS are in good agreement with those determined by atomicf orce microscopy (AFM), transmission electron microscopy (TEM), andd ynamic light scattering (DLS). In particular,t he SAXS data revealed important structurali nformation on these DNA nanotubes, such as the in-solution diameters ( % 25 nm), which could be obtained only with difficulty by use of other methods. Our resultsestablish SAXS as areliable structural analysism ethod for long DNA nanotubes and could assist in the rational design of these structures.Genetically encoded nanotubes made from biomacromolecules, such as cytoskeletal filaments, [1] channeling protein nanotubes, [2] and membrane channels, [3] are critical cellular components. They provide structural support for intracellular transport, intercellularc ommunication, and transmembrane ion/molecule channeling. [4,5] Inspired by the natural protein nanotubes widely encountered in vivo, in vitro construction of biomimetic DNA nanotubes has attracted growing interest with the development of structuralD NA nanotechnology. [6][7][8][9][10] In general, at ypical DNA nanotube can be fabricated either by parallel alignmento fD NA duplexes or throughw rapping of DNA tile lattices. [11][12][13] These biomimetic DNA nanotubes have shown great potentiali nawide number of areas, such as cargo delivery, [14] templated arrangement of other materials, artificial membrane channels, and nanoscale reaction containers.Although severalD NA nanotubes have been successfully createdb yu sing rational design, little is knowna bout their structures in solution.C urrently employed characterization methods generally rely on atomic force microscopy (AFM) or transmission electron microscopy (TEM), [15][16][17][18][19] which cannoti nterprett he in situ status of DNA nanotubes very well. Synchrotron small-angle X-ray scattering (SAXS), however,has emerged as ap owerful tool for in situ analysis of DNA nanostructures, especially for DNA nanotubes. SAXS has been used to study the interhelical spacingo fa24-helixb undle of DNA origami and the globalt wisting of planar DNA origami into nanotubes. [20,21] Further,t he positioning of chiral gold nanoparticles (AuNPs) decorated on ...

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Prokaryotic cytoskeletons: protein filaments organizing small cells

Cited by 109 publications

References 183 publications

DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth

DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth

Gain‐of‐function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling

In‐Situ Configuration Studies on Segmented DNA Origami Nanotubes

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