The Bacterial Cytoskeleton

Cabeen, Matthew T.; Jacobs‐Wagner, Christine

doi:10.1146/annurev-genet-102108-134845

Cited by 134 publications

(103 citation statements)

References 191 publications

(336 reference statements)

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“…Bacteria produce homologs of eukaryotic proteins that form filamentous structures, such as actin and tubulin. It is tempting to speculate that these proteins, which form the bacterial cytoskeleton, 19 are involved in targeting proteins to their sub-cellular destinations. particular positions where their future protein products are required.…”

Section: How Are Bacterial Proteins Targeted To Their Destination?mentioning

confidence: 99%

The compartmentalized vessel

2011

Cellular Logistics

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Section: How Are Bacterial Proteins Targeted To Their Destination?mentioning

confidence: 99%

The compartmentalized vessel

2011

Cellular Logistics

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“…During bacterial growth, peptidoglycan synthesis and deposition does not occur in a random fashion but is highly organized and localized to specific sites identified by cytoskeletal scaffolding proteins. In a typical rod-shaped bacterium, such as Bacillus subtilis, there are two phases of nascent peptidoglycan synthesis: during cell division at a midcell division site, where the primary cytoskeletal scaffold is provided by the tubulin-like FtsZ, and during elongation at the lateral wall, where members of the actin-like MreB family, including MreB, Mbl, and MreBH, are implicated in forming the helical pattern of nascent peptidoglycan synthesis (3). In spherical cells such as those of Staphylococcus aureus, only the FtsZ-driven cell wall synthesis takes place and occurs at the division site (4), whereas the curved rod-shaped bacterium Caulobacter crescentus also employs a third, intermediate filamentlike cytoskeletal protein, CreS, to establish its crescent shape (5,6).…”

mentioning

confidence: 99%

Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth inStreptomyces

Holmes¹,

Walshaw

Leggett³

et al. 2013

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

146

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Polarized growth in eukaryotes requires polar multiprotein complexes. Here, we establish that selection and maintenance of cell polarity for growth also requires a dedicated multiprotein assembly in the filamentous bacterium, Streptomyces coelicolor. We present evidence for a tip organizing center and confirm two of its main components: Scy (Streptomyces cytoskeletal element), a unique bacterial coiled-coil protein with an unusual repeat periodicity, and the known polarity determinant DivIVA. We also establish a link between the tip organizing center and the filamentforming protein FilP. Interestingly, both deletion and overproduction of Scy generated multiple polarity centers, suggesting a mechanism wherein Scy can both promote and limit the number of emerging polarity centers via the organization of the Scy-DivIVA assemblies. We propose that Scy is a molecular "assembler," which, by sequestering DivIVA, promotes the establishment of new polarity centers for de novo tip formation during branching, as well as supporting polarized growth at existing hyphal tips.bacterial polarized growth | polar multiprotein assembly | cell division | modified hendecad coiled coil H ow organisms, cells, or tissues establish polarity is one of the fundamental questions in developmental biology. In eukaryotes, from unicellular organisms to multicellular plants and animals, some of the core mechanisms for generating polarity are conserved (1). Sites for polarization must be selected using positional markers, followed by the recruitment of a complex assembly, which, in turn, orients cytoskeletal filaments that deliver vesicles to the particular sites. A specific example of polarity is polarized growth, during which cells select a single polarization site and generate elongated, cylindrical shapes, such as neuronal dendrites in animals, root hairs and pollen tubes in plants, hyphal growth of filamentous fungi, elongation of Schizosaccharomyces pombe, or the short period of polarized growth during budding in Saccharomyces cerevisiae. However, the presumed earliest examples of polarized growth can be found in bacteria. These include the actinomycete Streptomyces coelicolor, which is used as a model organism for studying morphological differentiation and filamentous growth.The complex life cycle of S. coelicolor begins with an ovoid spore that contains a single chromosome. During germination, long, multigenomic filaments (germ tubes) are formed, which branch regularly to generate a network of hyphal filaments. Branching is a necessity for exponential growth because the rate of tip elongation cannot exceed a certain maximum; hence, there is an exponential increase in the number of new tips. New tips develop on the lateral wall well behind the existing tip, a phenomenon also observed and described as apical dominance in eukaryotic filamentous fungi. When grown on semisolid agar medium, these hyphal filaments first grow across and into the solid medium, generating the vegetative mycelium, followed by the formation of an aerial mycelium by h...

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“…Various studies proved the existence of bacterial homologs of eukaryotic cytoskeleton proteins including tubulin homologs such as FtsZ (1), actin homologs such as MreB (2), and intermediate filament (IF)-like proteins (3), which together have important roles in cell division, morphogenesis, polarity determination, and DNA segregation (4)(5)(6)(7). In addition, several groups of polymer-forming proteins that are limited to the bacterial domain have been described (6).…”

mentioning

confidence: 99%

β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR

Vasa¹,

Lin

Shi

et al. 2014

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

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Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central conserved domain (DUF583) that is flanked by variable terminal regions. Here, we present a detailed investigation of bactofilin filaments from Caulobacter crescentus by highresolution solid-state NMR spectroscopy. De novo sequential resonance assignments were obtained for residues Ala39 to Phe137, spanning the conserved DUF583 domain. Analysis of the secondary chemical shifts shows that this core region adopts predominantly β-sheet secondary structure. Mutational studies of conserved hydrophobic residues located in the identified β-strand segments suggest that bactofilin folding and polymerization is mediated by an extensive and redundant network of hydrophobic interactions, consistent with the high intrinsic stability of bactofilin polymers. Transmission electron microscopy revealed a propensity of bactofilin to form filament bundles as well as sheet-like, 2D crystalline assemblies, which may represent the supramolecular arrangement of bactofilin in the native context. Based on the diffraction pattern of these 2D crystalline assemblies, scanning transmission electron microscopy measurements of the mass per length of BacA filaments, and the distribution of β-strand segments identified by solid-state NMR, we propose that the DUF583 domain adopts a β-helical architecture, in which 18 β-strand segments are arranged in six consecutive windings of a β-helix.solid-state NMR | cytoskeleton | protein structure | filaments

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The Bacterial Cytoskeleton

Cited by 134 publications

References 191 publications

The compartmentalized vessel

The compartmentalized vessel

Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth inStreptomyces

β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR

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