Entropy-driven translocation of disordered proteins through the Gram-positive bacterial cell wall
| Autor: | Nenad S. Mitić, Fabian E. Ortega, Julie A. Theriot, Ajay Gopinathan, Katharine M. Ng, Saša N. Malkov, Kerwyn Casey Huang, Matthew J. Footer, David K. Halladin |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Microbiology (medical)
Entropy Immunology Gram-Positive Bacteria Applied Microbiology and Biotechnology Microbiology Bacterial cell structure Article Cell wall 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Cell Wall Genetics Nuclear pore Cellular compartment Actin 030304 developmental biology 0303 health sciences 030306 microbiology Cell Biology Periplasmic space Transmembrane protein Transport protein Protein Transport chemistry Biophysics Peptidoglycan Cell envelope Entropy (order and disorder) |
| Zdroj: | Nat Microbiol |
| Popis: | Cells across all kingdoms of life actively partition molecules between discrete cellular compartments. In Gram-positive bacteria, a thick and highly cross-linked peptidoglycan cell wall separates the bacterial membrane from the extracellular space, imposing a barrier that must be crossed by proteins whose functions require that they be exposed on the bacterial cell surface1,2. Some surface-exposed proteins, such as the Listeria monocytogenes actin nucleation-promoting factor ActA3, remain associated with the bacterial membrane yet somehow thread through tens of nanometers of dense, cross-linked cell wall to expose their N-terminus on the outer surface4,5. Here, we show that entropy can drive the translocation of disordered transmembrane proteins through the Gram-positive cell wall. We develop a physical model predicting that the entropic constraint imposed by a thin periplasm is sufficient to drive translocation of an intrinsically disordered protein like ActA across a porous barrier similar to the cell wall. Consistent with this scenario, we demonstrate experimentally that translocation depends on both the dimensions of the cell envelope and the length of the disordered protein, and that translocation is reversible. We also show that disordered regions from eukaryotic nuclear pore complex proteins are capable of entropy-driven translocation through Gram-positive cell walls. These observations suggest that entropic forces alone, rather than chaperones or chemical energy, are sufficient to drive translocation of certain Gram-positive surface proteins for exposure on the outer surface of the cell wall. |
| Databáze: | OpenAIRE |
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