From Magnetosomes to Vesicles: LemA Proteins as Drivers of Bacterial Membrane Reorganization
- 1Technical University Braunschweig
Abstract
The cellular machineries that remodel bacterial membranes during organelle and vesicle formation remain poorly defined. Herein, we report MamQ as a key determinant of the lipid invaginations that enclose the magnetosome. MamQ belongs to the broadly conserved LemA protein family, whose members localize to either the inner or outer membrane. Heterologous overproduction of 13 different LemA proteins in Escherichia coli induced extensive membrane restructuring and vesiculation, indicating a conserved membrane-remodelling activity. In Pseudomonas aeruginosa, overproduction of the inner membrane protein LemA1 (PaLemA1) promoted cytoplasmic membrane vesicle (CMV) formation, whereas the periplasmic-located outer membrane-anchored LemA2 (PaLemA2) drove the formation of bacterial outer-membrane vesicles (OMVs). Conversely, deletion of the corresponding genes reduced extracellular vesicle production. Interactome analyses identified 256 protein partners of PaLemA1 and PaLemA2, including multiple components of the cellular divisome, such as CpoB, FtsE, FtsI, FtsK, FtsN, FtsW, MinE, ParB, ZapG, ZipA. Bacterial two-hybrid assays confirmed interactions between both LemA proteins and the cell division regulator CpoB, whose perturbation markedly altered vesicle formation. Additional interaction partners included PspA, an ESCRT-III-like protein implicated in membrane remodelling. Proteins involved in cell wall metabolism, membrane turnover, lipopolysaccharide (LPS) biogenesis, protein export and maturation, energy metabolism, and stress-responsive gene regulation were also enriched, suggesting a supporting role for PaLemA proteins in coordinating membrane-associated processes. Consistent with this, LemA deletion mutants displayed altered vesicle composition and global changes in gene expression. Furthermore, PalemA2 expression was induced in stationary phase and under envelope stress via the extracytoplasmic sigma factor AlgU, itself an interaction partner of the LemA proteins. Together, our findings indicate the LemA family act as a conserved membrane-remodelling system that, in conjunction with PspA, CpoB and divisome components, organises membrane-localized protein complexes required for bacterial organelle biogenesis and vesicle formation while executing a controlled, protein-machinery-driven mechanism that operates independently of passive chemical blebbing (such as hydrophobic PQS intercalation) or lytic membrane fragmentation.
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BibTeX
@misc{acuna2026from,
title = {{From Magnetosomes to Vesicles: LemA Proteins as Drivers of Bacterial Membrane Reorganization}},
author = {J. M. Borrero de Acuna and S. Holland and R. Juodeikis and A. Arce-Rodriguez and P. Ayala Garcia and M. Safa Karagoz and J. Giner-Lamia and G. Molinari and G. Deimantaviciute and V. Otto and C. Azogue-Palma and I. R. Brown and K. Muller and M. Jahn and K. E. Rennhack and S. Haussler and M. Rohde and L. Jansch and M. van Ham and M. Musken and E. Deery and C. M. Smales and M. Neumann-Schaal and M. J. Warren and D. Jahn},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.21.759321},
url = {https://www.biorxiv.org/content/10.64898/2026.10.21.759321v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - From Magnetosomes to Vesicles: LemA Proteins as Drivers of Bacterial Membrane Reorganization
AU - J. M. Borrero de Acuna
AU - S. Holland
AU - R. Juodeikis
AU - A. Arce-Rodriguez
AU - P. Ayala Garcia
AU - M. Safa Karagoz
AU - J. Giner-Lamia
AU - G. Molinari
AU - G. Deimantaviciute
AU - V. Otto
AU - C. Azogue-Palma
AU - I. R. Brown
AU - K. Muller
AU - M. Jahn
AU - K. E. Rennhack
AU - S. Haussler
AU - M. Rohde
AU - L. Jansch
AU - M. van Ham
AU - M. Musken
AU - E. Deery
AU - C. M. Smales
AU - M. Neumann-Schaal
AU - M. J. Warren
AU - D. Jahn
PY - 2026
DA - 2026/10/21
PB - bioRxiv
DO - 10.64898/2026.10.21.759321
UR - https://www.biorxiv.org/content/10.64898/2026.10.21.759321v1
AB - The cellular machineries that remodel bacterial membranes during organelle and vesicle formation remain poorly defined. Herein, we report MamQ as a key determinant of the lipid invaginations that enclose the magnetosome. MamQ belongs to the broadly conserved LemA protein family, whose members localize to either the inner or outer membrane. Heterologous overproduction of 13 different LemA proteins in Escherichia coli induced extensive membrane restructuring and vesiculation, indicating a conserved membrane-remodelling activity. In Pseudomonas aeruginosa, overproduction of the inner membrane protein LemA1 (PaLemA1) promoted cytoplasmic membrane vesicle (CMV) formation, whereas the periplasmic-located outer membrane-anchored LemA2 (PaLemA2) drove the formation of bacterial outer-membrane vesicles (OMVs). Conversely, deletion of the corresponding genes reduced extracellular vesicle production. Interactome analyses identified 256 protein partners of PaLemA1 and PaLemA2, including multiple components of the cellular divisome, such as CpoB, FtsE, FtsI, FtsK, FtsN, FtsW, MinE, ParB, ZapG, ZipA. Bacterial two-hybrid assays confirmed interactions between both LemA proteins and the cell division regulator CpoB, whose perturbation markedly altered vesicle formation. Additional interaction partners included PspA, an ESCRT-III-like protein implicated in membrane remodelling. Proteins involved in cell wall metabolism, membrane turnover, lipopolysaccharide (LPS) biogenesis, protein export and maturation, energy metabolism, and stress-responsive gene regulation were also enriched, suggesting a supporting role for PaLemA proteins in coordinating membrane-associated processes. Consistent with this, LemA deletion mutants displayed altered vesicle composition and global changes in gene expression. Furthermore, PalemA2 expression was induced in stationary phase and under envelope stress via the extracytoplasmic sigma factor AlgU, itself an interaction partner of the LemA proteins. Together, our findings indicate the LemA family act as a conserved membrane-remodelling system that, in conjunction with PspA, CpoB and divisome components, organises membrane-localized protein complexes required for bacterial organelle biogenesis and vesicle formation while executing a controlled, protein-machinery-driven mechanism that operates independently of passive chemical blebbing (such as hydrophobic PQS intercalation) or lytic membrane fragmentation.
ER -