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Structure paper

TitleLipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7472, Year 2025
Publish dateAug 12, 2025
AuthorsNathan Will / Giorgos Hiotis / Yoshitaka Nakayama / Gabriella Angiulli / Zijing Zhou / Charles D Cox / Boris Martinac / Thomas Walz /
PubMed AbstractYnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been ...YnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been extensively studied for MscS, but are less well understood for YnaI, which features two additional transmembrane helices. Here, we combined cryogenic electron microscopy, molecular dynamics simulations and patch-clamp electrophysiology to advance our understanding of YnaI. The two additional helices move the lipid-filled hydrophobic pockets in YnaI further away from the lipid bilayer and change the function of the pocket lipids from being a critical gating element in MscS to being more of a structural element in YnaI. Unlike MscS, YnaI shows pronounced gating hysteresis and remains open to a substantially lower membrane tension than is needed to initially open the channel. Thus, at near-lytic membrane tension, both MscL and YnaI will open, but while MscL has a large pore and must close quickly to minimize loss of essential metabolites, YnaI only conducts ions and can thus remain open for longer to continue to facilitate pressure equilibration across the membrane.
External linksNat Commun / PubMed:40796571 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.0 Å
Structure data

47547

9e62

EMDB-47547, PDB-9e62:
Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs
Method: EM (single particle) / Resolution: 2.5 Å

47548

9e63

EMDB-47548, PDB-9e63:
Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs treated with beta-cyclodextrin
Method: EM (single particle) / Resolution: 2.3 Å

47549

9e64

EMDB-47549, PDB-9e64:
Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs treated with lysophosphatidylcholine
Method: EM (single particle) / Resolution: 3.0 Å

47550

9e65

EMDB-47550, PDB-9e65:
Cryo-EM structure of mechanosensitive channel YnaI A155V mutant in conformation 1
Method: EM (single particle) / Resolution: 2.8 Å

47551

9e66

EMDB-47551, PDB-9e66:
Cryo-EM structure of mechanosensitive channel YnaI A155V mutant in conformation 2
Method: EM (single particle) / Resolution: 2.8 Å

47552

9e67

EMDB-47552, PDB-9e67:
Cryo-EM structure of mechanosensitive channel YnaI in DDPC nanodiscs
Method: EM (single particle) / Resolution: 2.3 Å

47553

9e68

EMDB-47553, PDB-9e68:
Cryo-EM structure of MscS/YnaI chimera in DOPC nanodiscs
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / Mechanosensitive

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