Cell division protein FtsK coordinates bacterial chromosome segregation and daughter cell separation in <i>Staphylococcus aureus</i>

Veiga, Helena; Jousselin, Ambre; Schäper, Simon; Saraiva, Bruno M; Marques, Leonor B; Reed, Patricia; Wilton, Joana; Pereira, Pedro M.; Filipe, Sérgio R.; Pinho, Mariana G.

doi:10.15252/embj.2022112140

Cited by 10 publications

(3 citation statements)

References 68 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…essentially performed as previously described 46 . Briefly, cells of strains JE2 and JE2 FtsZ(T111A) were grown in TSB rich medium at 37°C to mid-exponential phase (OD 600 of 0.6-0.8) and harvested by centrifugation.…”

Section: Transmission Electron Microscopy Transmission Electron Micro...mentioning

confidence: 99%

Processive movement ofStaphylococcus aureusessential septal peptidoglycan synthases is independent of FtsZ treadmilling and drives cell constriction

Schäper,

Brito,

Saraiva

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

Bacterial cell division is mediated by the tubulin-homolog FtsZ, which recruits peptidoglycan (PG) synthesis enzymes to the division site. Septal PG synthases promote inward growth of the division septum, but the mechanisms governing the spatiotemporal regulation of these enzymes are poorly understood. Recent studies on various organisms have proposed different models for the relationship between the movement and activity of septum-specific PG synthases and FtsZ treadmilling. Here, we studied the movement dynamics of conserved cell division proteins relative to the rates of septum constriction and FtsZ treadmilling in the Gram-positive pathogenStaphylococcus aureus. The septal PG synthesis enzyme complex FtsW/PBP1 and its putative activator protein, DivIB, moved processively, around the division site, with the same velocity. Impairing FtsZ treadmilling did not affect FtsW and DivIB velocities or septum constriction rates. Contrarily, inhibition of PG synthesis slowed down or completely stopped both septum constriction and the directional movement of FtsW/PBP1 and DivIB. Our findings support a model forS. aureusin which a single population of processively moving FtsW/PBP1 remains associated with DivIB to drive cell constriction independently of treadmilling FtsZ filaments.

show abstract

Section: Transmission Electron Microscopy Transmission Electron Micro...mentioning

confidence: 99%

Processive movement ofStaphylococcus aureusessential septal peptidoglycan synthases is independent of FtsZ treadmilling and drives cell constriction

Schäper,

Brito,

Saraiva

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…Autolytic enzymes affect both cell morphology and the cell cycle progression. In S. aureus, deletion of Atl and Sle1 autolysins leads to elongation of the cell cycle (Monteiro et al, 2015) while Sle1inactivation also causes a delay in cell daughter separation, resulting in an increase in cell size similarity to what is observed in the absence of MspA (Monteiro et al, 2015;Thalsø-Madsen et al, 2020;Veiga et al, 2023). An atl deletion mutant, in contrast, exhibits initiation of new septa before the previous round of cell division is completed, resulting in disturbed cell separation and cell clumping (Biswas et al, 2006;Chan et al, 2016;Nega et al, 2020).…”

Section: Discussionmentioning

confidence: 99%

Lipoteichoic acid biosynthesis byStaphylococcus aureusis controlled by the MspA protein through competitive interference

Bonini

Duggan

Al-Nahari

et al. 2023

Preprint

View full text Add to dashboard Cite

Staphylococcus aureus produces a plethora of virulence factors critical to its ability to establish an infection and cause disease. We have previously characterised a small membrane protein, MspA, which has pleiotropic affects on virulence and contributes to S. aureus pathogenicity in vivo. Here we report that mspA inactivation triggers overaccumulation of the essential cell wall component lipoteichoic acid (LTA) which, in turn, decreases autolytic activity and leads to increased cell size due to a delay in cell separation. We show that MspA directly interacts with the LTA synthesis enzymes UgtP, LtaA and LtaS, and competitively interferes with the association between LtaA and LtaS. While complementation of the mspA mutant with wild-type mspA reduces the amount of LTA, expression of a mutated version of MspA that does not interfere with the interactions between LtaA and LtaS does not. We suggest that MspA contributes to maintaining a physiological level of LTA in the cell wall by interacting with the LTA synthetic enzymes. In conclusion, this study uncovers the critical role of the MspA protein in regulating cell envelope biosynthesis and pathogenicity.

show abstract

“…This system consists of the ParA ATPase, which belongs to the same ATPase family as MinD (58) (60). Recently it was described that Staphylococcus aureus trigger factor (TF) forms a gradient by interacting with the cell division protein FtsK, resulting in an increased TF concentration towards the septal region (61). How TF reduces its diffusion in S. aureus cells is still unclear but might be a consequence of the fact that the chaperone directly interacts with ribosomes (62), which diffuse much slower due to their size and association with mRNA and nascent polypeptide chains.…”

Section: Protein Gradients In Bacteriamentioning

confidence: 99%

Cyclical MinD membrane affinity differences are not necessary for MinD gradient formation inBacillus subtilis

Bohorquez,

Strahl,

Marenduzzo

et al. 2024

Preprint

View full text Add to dashboard Cite

Proteins can diffuse micrometers in seconds, yet bacterial cells are able to maintain stable protein gradients. The best studied bacterial protein gradient is the Min system ofEscherichia coli. In rod-shaped bacteria the MinCD proteins prevent formation of minicells by inhibiting FtsZ polymerization close to the cell poles. InE. colithese proteins oscillate between cell poles within a minute, resulting in an increased MinCD concentration at the poles. This oscillation is caused by the interaction between MinD and the protein MinE, which form an ATP-driven reaction-diffusion system, whereby the ATPase MinD cycles between a monomeric cytosolic and a dimeric membrane attached states.Bacillus subtilisalso has MinCD, but lacks MinE. In this case MinCD form a static gradient that requires the transmembrane protein MinJ, located at cell poles and cell division sites. A recent reaction-diffusion model was successful in recreating the MinD gradient inB. subtilis, assuming that MinD cycles between cytosol and membrane, like inE. coli. Here we show that the monomeric and dimeric states ofB. subtilisMinD have comparable membrane affinities, that MinD interacts with MinJ as a dimer, and that MinJ is not required for membrane localization of MinD. Based on these new findings we tested different models, using kinetic Monte Carlo simulations, and found that a difference in diffusion rate between the monomer and dimer, rather than a difference in membrane affinity, is important forB. subtilisMinCD gradient formation.IMPORTANCEProteins can diffuse micrometers in seconds, yet bacterial cells are able to maintain stable protein gradients. One of the best studied examples is the membrane associated MinD protein gradient inEscherichia coli. This oscillating gradient requires cycling of MinD between a monomeric cytosolic and a dimeric membrane attached state.Bacillus subtilisalso has a Min system, but in this case MinD forms a static gradient. Mathematical models have been successful in recreating the MinD gradient inB. subtilis, using anE. coli-like membrane attachment cycle of MinD. Here we show that, in contrast to theE. colisituation, the monomeric and dimeric state ofB. subtilisMinD have comparable membrane affinities. Using this and other information, we tested Monte Carlo simulations and found that a difference in diffusion rate between MinD monomer and dimer, rather than a difference in membrane affinity, is important for MinD gradient formation inB. subtilis.

show abstract

Cell division protein FtsK coordinates bacterial chromosome segregation and daughter cell separation in Staphylococcus aureus

Cited by 10 publications

References 68 publications

Processive movement ofStaphylococcus aureusessential septal peptidoglycan synthases is independent of FtsZ treadmilling and drives cell constriction

Processive movement ofStaphylococcus aureusessential septal peptidoglycan synthases is independent of FtsZ treadmilling and drives cell constriction

Lipoteichoic acid biosynthesis byStaphylococcus aureusis controlled by the MspA protein through competitive interference

Cyclical MinD membrane affinity differences are not necessary for MinD gradient formation inBacillus subtilis

Contact Info

Product

Resources

About