ArticleNature microbiology2021
Entropy-driven translocation of disordered proteins through the Gram-positive bacterial cell wall.
Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Article
- Wall teichoic acids regulate peptidoglycan synthesis to maintain rod shape in Bacillus subtilis.Nature microbiology · 2026Article
- Proximity labeling of thebioRxiv : the preprint server for biology · 2026Article
- A universal entropic pulling force caused by binding.Nature communications · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Systematic analysis of structural disorder in the minimal proteome ofMicrobiology spectrum · 2025Article
- Cyclic-di-AMP modulates cellular turgor in response to defects in bacterial cell wall synthesis.Nature microbiology · 2025Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Streamlining N-terminally anchored yeast surface display via structural insights into S. cerevisiae Pir proteins.Microbial cell factories · 2023Article
- Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles.The journal of physical chemistry. B · 2023Article
- Article
- Structural preferences shape the entropic force of disordered protein ensembles.bioRxiv : the preprint server for biology · 2023Article
- Article
- Threading single proteins through pores to compare their energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Fc-MBL-modified FeMikrochimica acta · 2022Article
- Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism.Frontiers in molecular biosciences · 2022Article
- Proteins sorted by 'chaos and disorder'.Nature microbiology · 2021Article
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Abstract
In Gram-positive bacteria, a thick cross-linked cell wall separates the membrane from the extracellular space. Some surface-exposed proteins, such as the Listeria monocytogenes actin nucleation-promoting factor ActA, remain associated with the bacterial membrane but somehow thread through tens of nanometres of cell wall to expose their amino terminus to the exterior. Here, we report that entropy enables the translocation of disordered transmembrane proteins through the Gram-positive cell wall. We build a physical model, which predicts that the entropic constraint imposed by a thin periplasm is sufficient to drive the translocation of an intrinsically disordered protein such as ActA across a porous barrier similar to a peptidoglycan cell wall. We experimentally validate our model and show that ActA translocation depends on the cell-envelope dimensions and disordered-protein length, and that translocation is reversible. We also show that disordered regions of eukaryotic proteins can translocate Gram-positive cell walls via entropy. We propose that entropic forces are sufficient to drive the translocation of specific proteins to the outer surface.
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