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Peer-reviewedCC BY 4.0Environmental Microbiology

An SPFH Protein Couples Membrane Stress to Differentiation in Bacillus subtilis

  • Sarah S. M. Baur1
  • Urška Repnik2
  • Tobias Busche3
  • Louisa Rau1
  • Alisa Mondry1,4
  • Marc Bramkamp1,2
4 affiliations
  1. 1Christian‐Albrechts‐Universität zu Kiel, Mathematisch‐Naturwissenschaftliche Fakultät Institut für Allgemeine Mikrobiologie Kiel Germany
  2. 2Christian‐Albrechts‐Universität zu Kiel, Mathematisch‐Naturwissenschaftliche Fakultät Zentrale Mikroskopie Kiel Germany
  3. 3Bielefeld University Medical School OWL & Center for Biotechnology (CeBiTec) Bielefeld Germany
  4. 4MRC Laboratory of Molecular Biology Cambridge UK
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Abstract

Bacillus subtilis adapts to fluctuating environmental stress, such as membrane perturbation or alkaline conditions, using membrane‐associated regulatory complexes. Here, we rename the previously termed pspA‐ydjGHI operon to pspA‐samGHI (for starvation and motility) to reflect its functional roles. The membrane proteins SamG and SamH recruit SamI, a cytosolic SPFH (Stomatin/Prohibitin/Flotillin/HflK‐C) protein that coordinates the recruitment of PspA, an ESCRT‐III homologue from a protein family involved in membrane repair and remodelling. Here we show that SamGHI impacts developmental processes, allowing proper motility, secretion, and colony biofilm formation in the laboratory B. subtilis strain WT168. Loss of SamI (ΔsamI/ΔydjI) leads to unbalanced SamH activity, resulting in global transcriptional changes reminiscent of starvation situations. This, in turn, reduces secretion of the matrix protein BslA, preventing colony biofilm formation. Deletion of samH in combination with ΔsamI restores colony morphology, while ΔpspA mutants form normal colonies, indicating that PspA is dispensable for the developmental phenotype. Our findings reveal that, beyond its role in maintaining membrane integrity, SamGHI influences the cellular physiological state and thereby impacts multicellular development.

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Cite

BibTeXRIS
BibTeX
@article{baur2026spfh,
  title = {{An SPFH Protein Couples Membrane Stress to Differentiation in Bacillus subtilis}},
  author = {Sarah S. M. Baur and Urška Repnik and Tobias Busche and Louisa Rau and Alisa Mondry and Marc Bramkamp},
  journal = {Environmental Microbiology},
  year = {2026},
  month = oct,
  doi = {10.1111/1462-2920.70467},
  url = {https://doi.org/10.1111/1462-2920.70467},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - An SPFH Protein Couples Membrane Stress to Differentiation in Bacillus subtilis
AU  - Sarah S. M. Baur
AU  - Urška Repnik
AU  - Tobias Busche
AU  - Louisa Rau
AU  - Alisa Mondry
AU  - Marc Bramkamp
PY  - 2026
DA  - 2026/10/27
JO  - Environmental Microbiology
DO  - 10.1111/1462-2920.70467
UR  - https://doi.org/10.1111/1462-2920.70467
AB  - Bacillus subtilis adapts to fluctuating environmental stress, such as membrane perturbation or alkaline conditions, using membrane‐associated regulatory complexes. Here, we rename the previously termed pspA‐ydjGHI operon to pspA‐samGHI (for starvation and motility) to reflect its functional roles. The membrane proteins SamG and SamH recruit SamI, a cytosolic SPFH (Stomatin/Prohibitin/Flotillin/HflK‐C) protein that coordinates the recruitment of PspA, an ESCRT‐III homologue from a protein family involved in membrane repair and remodelling. Here we show that SamGHI impacts developmental processes, allowing proper motility, secretion, and colony biofilm formation in the laboratory B. subtilis strain WT168. Loss of SamI (ΔsamI/ΔydjI) leads to unbalanced SamH activity, resulting in global transcriptional changes reminiscent of starvation situations. This, in turn, reduces secretion of the matrix protein BslA, preventing colony biofilm formation. Deletion of samH in combination with ΔsamI restores colony morphology, while ΔpspA mutants form normal colonies, indicating that PspA is dispensable for the developmental phenotype. Our findings reveal that, beyond its role in maintaining membrane integrity, SamGHI influences the cellular physiological state and thereby impacts multicellular development.
SN  - 1462-2912
SN  - 1462-2920
ER  -