An Stomatin, Prohibitin, Flotillin, and HflK/C-Domain Protein Required to Link the Phage-Shock Protein to the Membrane in Bacillus subtilis

Scholz, Abigail Savietto; Baur, Sarah S. M.; Wolf, Diana; Bramkamp, Marc

doi:10.3389/fmicb.2021.754924

Cited by 10 publications

(12 citation statements)

References 70 publications

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“…In Bacillus subtilis , the flotillin-like protein YdjI has recently been shown to be key to localization of the inner-membrane remodeler phage shock protein A, for which there are two orfs in Ca . T. nelsonii genomes [79].…”

Section: Discussionmentioning

confidence: 99%

Outside-in: intracellular vesicles in giant sulfur bacteria contain peptidoglycan

Flood

Leprich

Hunter

et al. 2022

Preprint

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Until recently, the cellular envelopes of bacteria were regarded as static and rigid relative to those of eukaryotes. While investigating peptidoglycan synthesis in populations of giant sulfur bacteria, Candidatus Thiomargarita spp., we observed internal vesicle-like features (VLFs). VLFs, as imaged following the active incorporation of D-amino acids, appear to begin as invaginations and delaminations of the cellular envelope. Staining with wheat germ agglutinin confirmed the presence of peptidoglycan in VLFs, while polymyxin B revealed that the outer membrane is present in some VLFs. Transmission electron microscopy revealed a complex network of interconnected VLFs. Genomes of Ca . Thiomargarita nelsonii lack a canonical divisome, while possessing homologs to genes such as actin, membrane scaffolding proteins, and dynamins that are associated with phagocytosis in eukaryotes. The physiological role of VLFs remains unclear, but the presence of sulfur globules in some suggests compartmentalization of metabolism and energy production. This is the first report of peptidoglycan and outer membrane bound intracellular vesicles within prokaryotic cells. These findings transform the canonical view of the inflexible bacterial cell envelope and further narrow the divide between prokaryotes and eukaryotes.

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Section: Discussionmentioning

confidence: 99%

Outside-in: intracellular vesicles in giant sulfur bacteria contain peptidoglycan

Flood

Leprich

Hunter

et al. 2022

Preprint

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“…In Bacillus subtilis, the flotillins FloA and FloT are discussed to functionally organize the bacterial membrane via the formation of microdomains (123), which appear to be important for transmembrane signal transduction and transport processes. The Bacillus subtilis flotillin YdjH has been shown to be involved in the recruitment of the bacterial ESCRT-III protein PspA (discussed later) to membranes, which is part of a membrane stress response system involved in bacterial membrane protection (124). Noteworthy, expression of the genes coding for Bacillus subtilis flotillines is genetically regulated by the stress-responsive ECF sigma factor σ w , indicating that flotillines also have stress-responsive, membrane-remodeling and/or -stabilizing functions rather than just Downloaded from http://portlandpress.com/bioscirep/article-pdf/doi/10.1042/BSR20221269/941683/bsr-2022-1269c.pdf by guest on 16 January 2023 being involved in the formation of defined membrane domains (125).…”

Section: Lateral Lipid Asymmetrymentioning

confidence: 99%

Cyanobacterial membrane dynamics in the light of eukaryotic principles

Siebenaller

Schneider

2023

Bioscience Reports

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Intracellular compartmentalization is a hallmark of eukaryotic cells. Dynamic membrane remodeling, involving membrane fission/fusion events, clearly is crucial for cell viability and function, as well as membrane stabilization and/or repair, e.g., during or after injury. In recent decades, several proteins involved in membrane stabilization and/or dynamic membrane remodeling have been identified and described in eukaryotes. Yet, while typically not having a cellular organization as complex as eukaryotes, also bacteria can contain extra internal membrane systems besides the cytoplasmic membranes. Thus, also in bacteria mechanisms must have evolved to stabilize membranes and/or trigger dynamic membrane remodeling processes. In fact, in recent years proteins, which were initially defined being eukaryotic inventions, have been recognized also in bacteria, and likely these proteins shape membranes also in these organisms. One example of a complex prokaryotic inner membrane system is the thylakoid membrane of cyanobacteria, which contains the complexes of the photosynthesis light reaction. Cyanobacteria are evolutionary closely related to chloroplasts, and extensive remodeling of the internal membrane systems has been observed in chloroplasts and cyanobacteria during membrane biogenesis and/or at changing light conditions. We here discuss common principles guiding eukaryotic and prokaryotic membrane dynamics and the proteins involved, with a special focus on the dynamics of the cyanobacterial thylakoid and cytoplasmic membranes.

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“…3b). YdjI is a stomatin, prohibitin, flotillin, and HflK/C-domain protein which localizes into liquid disordered membrane regions, and homologs assemble into higher oligomeric structures [32][33][34] .…”

Section: The Bce Cyclase Is Conjugated To Phage Shock Protein Amentioning

confidence: 99%

“…3b). It has been described that PspA proteins assemble in helical rods with an ESCRT-III-like fold 36,37 , and such PspA foci have been observed in B. subtilis microscopically 7 32 . Thus, we hypothesize that the cyclase associates with and is conjugated to PspA rods in vivo.…”

Section: The Bce Cyclase Is Conjugated To Phage Shock Protein Amentioning

confidence: 99%

Reversible conjugation of a CBASS nucleotide cyclase regulates immune response to phage infection

Krüger,

Gaskell-Mew,

Graham

et al. 2023

Preprint

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Antiviral defence systems build the prokaryotic immune system and their proper regulation is vital for survival and fitness. While it is important that they are readily available in case of infection, they need to be tightly controlled to prevent activation of an unnecessary cellular response. Here we describe how the bacterial cyclic oligonucleotide-based antiphage signalling system (CBASS) uses its intrinsic protein modification system to regulate the nucleotide cyclase. By integrating a Type II CBASS system fromBacillus cereusinto the cognate hostBacillus subtilis, we show that the Cap2 protein conjugates the cyclase exclusively to the conserved phage shock protein A (PspA) in the absence of phage. This cyclase-PspA conjugation is reversed after infection by the isopeptidase Cap3. Finally, we propose a model in which the cyclase is held in an inactive state by conjugation to PspA in the absence of phage and that this conjugation is released upon infection, priming the cyclase for activation.

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An Stomatin, Prohibitin, Flotillin, and HflK/C-Domain Protein Required to Link the Phage-Shock Protein to the Membrane in Bacillus subtilis

Cited by 10 publications

References 70 publications

Outside-in: intracellular vesicles in giant sulfur bacteria contain peptidoglycan

Outside-in: intracellular vesicles in giant sulfur bacteria contain peptidoglycan

Cyanobacterial membrane dynamics in the light of eukaryotic principles

Reversible conjugation of a CBASS nucleotide cyclase regulates immune response to phage infection

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