Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions

Eun, Ye-Jin; Kapoor, Mrinal; Hussain, Saman; Garner, Ethan C.

doi:10.1074/jbc.r115.637876

Cited by 36 publications

(24 citation statements)

References 100 publications

(118 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is still not universally recognized how rigid the FtsZ pfs really are. For example, a recent review commented “ recent work has suggested that FtsZ filaments may be too flexible to bend membranes… ” (Eun et al 2015). Ramirez-Aportela et al (2014) commented on “ …the large disparity in measurements [of persistence length] found in the literature for GTP/GDP filaments of FtsZ from other species.…”

Section: Ftsz Pfs Are Mechanically Rigidmentioning

confidence: 99%

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

Erickson

Osawa

2017

Subcellular Biochemistry

View full text Add to dashboard Cite

FtsZ assembles in vitro into protofilaments (pfs) that are one subunit thick and ~50 subunits long. In vivo these pfs assemble further into the Z ring, which, along with accessory division proteins, constricts to divide the cell. We have reconstituted Z rings in liposomes in vitro, using pure FtsZ that was modified with a membrane targeting sequence to directly bind the membrane. This FtsZ-mts assembled Z rings and constricted the liposomes without any accessory proteins. We proposed that the force for constriction was generated by a conformational change from straight to curved pfs. Evidence supporting this mechanism came from switching the membrane tether to the opposite side of the pf. These switched-tether pfs assembled “inside-out” Z rings, and squeezed the liposomes from the outside, as expected for the bending model. We propose three steps for the full process of cytokinesis: (a) pf bending generates a constriction force on the inner membrane, but the rigid peptidoglycan wall initially prevents any invagination; (b) downstream proteins associate to the Z ring and remodel the peptidoglycan, permitting it to follow the constricting FtsZ to a diameter of ~250 nm; the final steps of closure of the septum and membrane fusion are achieved by excess membrane synthesis and membrane fluctuations.

show abstract

Section: Ftsz Pfs Are Mechanically Rigidmentioning

confidence: 99%

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

Erickson

Osawa

2017

Subcellular Biochemistry

View full text Add to dashboard Cite

show abstract

“…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%

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

et al. 2018

View full text Add to dashboard Cite

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.

show abstract

“…The system involved in cell division is governed by the bacterial tubulin FtsZ and the associated septation‐specific PBPs. The system involved in sidewall elongation is controlled by the Rod system, a system of morphogenetic proteins including the bacterial actin homologue MreB as well as MreC, MreD, RodA, RodZ and elongation‐specific PBPs (Eun et al ., 2015). One of the unexplained aspects of the Rod system in B. subtilis is that the lethality and/or morphological defects of the absence of some of its components can be overcome by adding Mg 2+ to the growth medium (Formstone and Errington, 2005).…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of peptidoglycan is modulated by amidation of meso‐diaminopimelic acid and Mg²⁺ in Bacillus subtilis

Dajkovic

Tesson

Chauhan

et al. 2017

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe ability of excess Mg2+ to compensate the absence of cell wall related genes in Bacillus subtilis has been known for a long time, but the mechanism has remained obscure. Here, we show that the rigidity of wild‐type cells remains unaffected with excess Mg2+, but the proportion of amidated meso‐diaminopimelic (mDAP) acid in their peptidoglycan (PG) is significantly reduced. We identify the amidotransferase AsnB as responsible for mDAP amidation and show that the gene encoding it is essential without added Mg2+. Growth without excess Mg2+ causes ΔasnB mutant cells to deform and ultimately lyse. In cell regions with deformations, PG insertion is orderly and indistinguishable from the wild‐type. However, PG degradation is unevenly distributed along the sidewalls. Furthermore, ΔasnB mutant cells exhibit increased sensitivity to antibiotics targeting the cell wall. These results suggest that absence of amidated mDAP causes a lethal deregulation of PG hydrolysis that can be inhibited by increased levels of Mg2+. Consistently, we find that Mg2+ inhibits autolysis of wild‐type cells. We suggest that Mg2+ helps to maintain the balance between PG synthesis and hydrolysis in cell wall mutants where this balance is perturbed in favor of increased degradation.

show abstract

Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions

Cited by 36 publications

References 100 publications

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

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

Hydrolysis of peptidoglycan is modulated by amidation of meso‐diaminopimelic acid and Mg²⁺ in Bacillus subtilis

Contact Info

Product

Resources

About

Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions

Cited by 36 publications

References 100 publications

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

FtsZ Constriction Force – Curved Protofilaments Bending Membranes

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

Hydrolysis of peptidoglycan is modulated by amidation of meso‐diaminopimelic acid and Mg2+ in Bacillus subtilis

Contact Info

Product

Resources

About

Hydrolysis of peptidoglycan is modulated by amidation of meso‐diaminopimelic acid and Mg²⁺ in Bacillus subtilis