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TitleFlotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5583, Year 2024
Publish dateJul 3, 2024
AuthorsMarta Ukleja / Lara Kricks / Gabriel Torrens / Ilaria Peschiera / Ines Rodrigues-Lopes / Marcin Krupka / Julia García-Fernández / Roberto Melero / Rosa Del Campo / Ana Eulalio / André Mateus / María López-Bravo / Ana I Rico / Felipe Cava / Daniel Lopez /
PubMed AbstractThe function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the ...The function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the biological function of these membrane microdomains remain unclear. Here, we show that FMMs in the pathogen methicillin-resistant Staphylococcus aureus (MRSA) are dedicated to confining and stabilizing proteins unfolded due to cellular stress. The FMM scaffold protein flotillin forms a clamp-shaped oligomer that holds unfolded proteins, stabilizing them and favoring their correct folding. This process does not impose a direct energy cost on the cell and is crucial to survival of ATP-depleted bacteria, and thus to pathogenesis. Consequently, FMM disassembling causes the accumulation of unfolded proteins, which compromise MRSA viability during infection and cause penicillin re-sensitization due to PBP2a unfolding. Thus, our results indicate that FMMs mediate ATP-independent stabilization of unfolded proteins, which is essential for bacterial viability during infection.
External linksNat Commun / PubMed:38961085 / PubMed Central
MethodsEM (single particle)
Resolution7.9 - 8.0 Å
Structure data

EMDB-17217: Structure of Staphylococcus aureus FloA protein
Method: EM (single particle) / Resolution: 8.0 Å

EMDB-17222: Structure of the FloA-NfeD complex
Method: EM (single particle) / Resolution: 7.9 Å

Source
  • Staphylococcus aureus subsp. aureus N315 (bacteria)
  • Staphylococcus (bacteria)

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