Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus

Woldemeskel, Selamawit Abi; Goley, Erin D.

doi:10.1016/j.tim.2017.03.006

Cited by 40 publications

(36 citation statements)

References 110 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Despite of the low 229 abundance of filaments, heterologous expression of YFP-Fm7001 induced a swollen 230 phenotype and the formation of Fischerella cell filaments that seemingly divided in more than 231 one plane (resembling the multiseriate Chlorogloeopsis fritschii PCC 6912 phenotype). This 232 effect suggests a contribution of Fm7001 in cell-size control in the true-branching phenotype 233 of Fischerella, reminiscent of crescentin or CtpS, (Woldemeskel and Goley, 2017). Attempts 234 to generate a ∆fm7001 mutant strain remained unsuccessful.…”

Section: While In 227mentioning

confidence: 99%

Identification and characterization of novel filament-forming proteins in cyanobacteria

Springstein

Woehle

Weißenbach

et al. 2019

Preprint

View full text Add to dashboard Cite

17Filament-forming proteins in the bacterial cytoskeleton function in stabilization and localization 18 of proteinaceous complexes and replicons. Research of the cyanobacterial cytoskeleton is 19 focused on the bacterial tubulin (FtsZ) and actin (MreB). Nonetheless, the diverse colony 20 morphologies and cell types in cyanobacteria suggest the presence of additional cytoskeletal 21 proteins. Here we present two novel filament-forming proteins in cyanobacteria. Surveying 22 cyanobacterial genomes for coiled-coil-rich proteins (CCRPs), we observed a higher 23 proportion of CCRPs in filamentous cyanobacteria in comparison to unicellular cyanobacteria. 24We identified nine protein families with putative intermediate filament (IF) properties. 25Polymerization assays revealed four polymer-forming proteins in vitro and three polymer-26 forming proteins in vivo. Fm7001 from Fischerella muscicola PCC 7414 polymerized in vitro 27 and formed filaments in different in vivo systems. Functional analysis of Fm7001 suggests that 28 it has IF-like properties. Additionally, we identified a tetratricopeptide repeat protein, All4981 in 29Anabaena sp. PCC 7120 that polymerized into filaments in vivo and in vitro. All4981 interacts 30 with other known cytoskeletal proteins and is indispensable for Anabaena. Our results expand 31 the repertoire of known prokaryotic filament-forming CCRPs and demonstrate that 32 cyanobacterial CCRPs are involved in cell morphology, motility, cytokinesis and colony 33 integrity. 34 Author Summary 35The phylum Cyanobacteria is characterized by a large morphological diversity, ranging from 36 coccoid or rod-shaped unicellular species to complex filamentous multicellular species. Many 37 species of multicellular cyanobacteria can undergo cell differentiation and changes in their cell 38 shape. Despite this diversity, very few molecular mechanisms underlying the cyanobacterial 39 morphological plasticity are known. Among these, the cytoskeletal proteins FtsZ and MreB are 40 important regulators of cyanobacterial cell shape and viability. Also, the multicellular phenotype 41 of filamentous cyanobacteria has been linked to prokaryotic gap-junction analogs, the septal 42 junctions. The significance of our research is the identification and characterization of a novel 43 3 cyanobacterial cytoskeletal repertoire of IF-like proteins that will aid in the characterization of 44 the morphological complexity of cyanobacteria. Thus, our survey leads to a broader 45 understanding of the underlying principles of cyanobacterial morphotypes and will serve as a 46 starting point for future research to further unravel the complex morphologies unique to this 47 phylum. 48

show abstract

Section: While In 227mentioning

confidence: 99%

Identification and characterization of novel filament-forming proteins in cyanobacteria

Springstein

Woehle

Weißenbach

et al. 2019

Preprint

View full text Add to dashboard Cite

show abstract

“…Indeed, it was possible to identify a few dividing cells with prosthecae of equal length ( Figure 2B ). Dynamic morphology change in a cell cycle is already known from other prosthecate bacteria, such as Caulobacter 53 and Asticcacaulis 54 .…”

Section: Resultsmentioning

confidence: 99%

Novel prosthecate bacteria from the candidate phylum Acetothermia revealed by culture-independent genomics and advanced microscopy

Hao

McIlroy

Kirkegaard

et al. 2017

Preprint

View full text Add to dashboard Cite

Members of the candidate phylum Acetothermia are globally distributed and detected in various habitats. However, little is known about their physiology and ecological importance. In this study, an OTU belonging to Acetothermia was detected at high abundance in two full-scale anaerobic digesters. The first closed genome from this phylum was obtained by differential coverage binning of metagenomes and scaffolding with nanopore data. Genome annotation and metabolic reconstruction suggested an anaerobic chemoheterotrophic lifestyle in which the bacterium obtain energy and carbon via fermentation of peptides, amino acids, and simple sugars to acetate, formate, and hydrogen. The morphology was unusual and composed of a central rod-shaped cell with bipolar prosthecae as revealed by fluorescence in situ hybridization combined with confocal laser scanning microscopy, Raman microspectroscopy and atomic force microscopy. We hypothesize that these prosthecae allow for increased nutrient uptake by greatly expanding the cell surface area, providing a competitive advantage under nutrient-limited conditions.

show abstract

“…This complex process requires recruitment at mid‐cell of the conserved protein FtsZ, a homolog of eukaryotic tubulin, while the protein FtsA is required for the recruitment of a large complex of division proteins (i.e. the divisome) that drives neosynthesis of the cell wall peptidoglycan (Lutkenhaus et al ., ; Xiao and Goley, ; Woldemeskel and Goley, ).…”

Section: Cell Envelope and Divisionmentioning

confidence: 99%

A new factor controlling cell envelope integrity in Alphaproteobacteria in the context of cell cycle, stress response and infection

Beroual

Biondi

2019

Molecular Microbiology

View full text Add to dashboard Cite

Summary The bacterial envelope is a remarkable and complex compartment of the prokaryotic cell in which many essential functions take place. The article by Herrou and collaborators (Herrou et al., in press), by a clever combination of structural analysis, genetics and functional characterization in free‐living bacterial cells and during infection in animal models, elucidates a new factor, named EipA, that plays a major role in Brucella spp envelope biogenesis and cell division. The authors demonstrate a genetic connection between eipA and lipopolysaccharide synthesis, specifically genes involved in the synthesis of the O‐antigen portion of lipopolysaccharide (LPS). Beyond its crucial role in Brucella physiology, the conservation of EipA in the class Alphaproteobacteria urges microbiologists to pursue future investigation of its homologs in other species belonging to this important group of bacteria.

show abstract

Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus

Cited by 40 publications

References 110 publications

Identification and characterization of novel filament-forming proteins in cyanobacteria

Identification and characterization of novel filament-forming proteins in cyanobacteria

Novel prosthecate bacteria from the candidate phylum Acetothermia revealed by culture-independent genomics and advanced microscopy

A new factor controlling cell envelope integrity in Alphaproteobacteria in the context of cell cycle, stress response and infection

Contact Info

Product

Resources

About