ArticlePLoS computational biology2021
The quantitative basis for the redistribution of immobile bacterial lipoproteins to division septa.
Article in PLoS computational biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Bacterial cell widening alters periplasmic size and activates envelope stress responses.The EMBO journal · 2025Article
- Origin and Evolution of Bacterial Periplasmic Force Transducers.Molecular biology and evolution · 2025Article
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- A molecular switch controls assembly of bacterial focal adhesions.Science advances · 2024Article
- Cell division cycle fluctuation of Pal concentration in Escherichia coli.Access microbiology · 2024Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Force-Generation by the Trans-Envelope Tol-Pal System.Frontiers in microbiology · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spatial localisation of proteins is critical for most cellular function. In bacteria, this is typically achieved through capture by established landmark proteins. However, this requires that the protein is diffusive on the appropriate timescale. It is therefore unknown how the localisation of effectively immobile proteins is achieved. Here, we investigate the localisation to the division site of the slowly diffusing lipoprotein Pal, which anchors the outer membrane to the cell wall of Gram-negative bacteria. While the proton motive force-linked TolQRAB system is known to be required for this repositioning, the underlying mechanism is unresolved, especially given the very low mobility of Pal. We present a quantitative, mathematical model for Pal relocalisation in which dissociation of TolB-Pal complexes, powered by the proton motive force across the inner membrane, leads to the net transport of Pal along the outer membrane and its deposition at the division septum. We fit the model to experimental measurements of protein mobility and successfully test its predictions experimentally against mutant phenotypes. Our model not only explains a key aspect of cell division in Gram-negative bacteria, but also presents a physical mechanism for the transport of low-mobility proteins that may be applicable to multi-membrane organelles, such as mitochondria and chloroplasts.
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