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TitleMechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7881, Year 2025
Publish dateAug 23, 2025
AuthorsVanessa J Flegler / Akiko Rasmussen / Rainer Hedrich / Tim Rasmussen / Bettina Böttcher /
PubMed AbstractOsmotically varying environments are challenging for bacterial cells. Sudden drops in osmolytes cause an increased membrane tension and rupture the cells in the absence of protective mechanisms. One ...Osmotically varying environments are challenging for bacterial cells. Sudden drops in osmolytes cause an increased membrane tension and rupture the cells in the absence of protective mechanisms. One family of protective proteins are mechanosensitive channels of small conductance that open in response to membrane tension. Although these channels have a common architecture, they vary widely in the number of transmembrane helices, conductivity, and gating characteristics. Although there are various structures of channels in the open and closed state, the underlying common principles of the gating mechanism remain poorly understood. Here we show that YnaI opens by radial relocation of the transmembrane sensor paddles together with a shortening of the pore, which contrasts the prototypic smaller MscS. A chimera of both channels with the YnaI sensor paddles and the pore containing C-terminal part of MscS is functional and has the tension response of the paddle donor. Our research shows that elements with different structural opening mechanisms can be mixed and matched within one channel as long as they support the common area expansion on the periplasmic side.
External linksNat Commun / PubMed:40849500 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 3.6 Å
Structure data

EMDB-51813, PDB-9h2p:
YnaI in its open conformation purified in DDM showing ligand-filled pockets
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-51817, PDB-9h2s:
a YnaI-MscS chimera in a closed conformation purified in DDM with additional lipids showing ligand-filled pore and pockets
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-51818, PDB-9h2v:
a YnaI-MscS chimera in an open conformation purified in DDM showing ligand-filled pockets
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-51897: YnaI in its open conformation, purified in DDM, C1 processed
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-51898: A YnaI-MscS chimera in its closed conformation, C1 processed
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-51953, PDB-9h95:
YnaI in closed conformation purified in DDM with additional lipids showing ligand-filled pockets
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-51954: A YnaI-MscS chimera in its open conformation, C1 processed
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-D12:
DODECANE

Source
  • escherichia coli (E. coli)
  • unidentified (others)
  • escherichia coli (strain k12) (bacteria)
KeywordsMEMBRANE PROTEIN / YnaI; mechanosensitive ion channel of E. coli; MscS-like / chimera; mechanosensitive ion channel; MscS-like / mechanosensitive ion channel of E. coli; MscS-like

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