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TitleMechanosensitive channel gating by delipidation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 33, Year 2021
Publish dateAug 17, 2021
AuthorsVanessa Judith Flegler / Akiko Rasmussen / Karina Borbil / Lea Boten / Hsuan-Ai Chen / Hanna Deinlein / Julia Halang / Kristin Hellmanzik / Jessica Löffler / Vanessa Schmidt / Cihan Makbul / Christian Kraft / Rainer Hedrich / Tim Rasmussen / Bettina Böttcher /
PubMed AbstractThe mechanosensitive channel of small conductance (MscS) protects bacteria against hypoosmotic shock. It can sense the tension in the surrounding membrane and releases solutes if the pressure in the ...The mechanosensitive channel of small conductance (MscS) protects bacteria against hypoosmotic shock. It can sense the tension in the surrounding membrane and releases solutes if the pressure in the cell is getting too high. The membrane contacts MscS at sensor paddles, but lipids also leave the membrane and move along grooves between the paddles to reside as far as 15 Å away from the membrane in hydrophobic pockets. One sensing model suggests that a higher tension pulls lipids from the grooves back to the membrane, which triggers gating. However, it is still unclear to what degree this model accounts for sensing and what contribution the direct interaction of the membrane with the channel has. Here, we show that MscS opens when it is sufficiently delipidated by incubation with the detergent dodecyl-β-maltoside or the branched detergent lauryl maltose neopentyl glycol. After addition of detergent-solubilized lipids, it closes again. These results support the model that lipid extrusion causes gating: Lipids are slowly removed from the grooves and pockets by the incubation with detergent, which triggers opening. Addition of lipids in micelles allows lipids to migrate back into the pockets, which closes the channel even in the absence of a membrane. Based on the distribution of the aliphatic chains in the open and closed conformation, we propose that during gating, lipids leave the complex on the cytosolic leaflet at the height of highest lateral tension, while on the periplasmic side, lipids flow into gaps, which open between transmembrane helices.
External linksProc Natl Acad Sci U S A / PubMed:34376558 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.9 Å
Structure data

12996

7onj

EMDB-12996, PDB-7onj:
Mechanosensitive channel MscS solubilized with LMNG in open conformation
Method: EM (single particle) / Resolution: 2.3 Å

12997

7onl

EMDB-12997, PDB-7onl:
Mechanosensitive channel MscS solubilized with DDM in closed conformation
Method: EM (single particle) / Resolution: 3.9 Å

13003

7oo0

EMDB-13003, PDB-7oo0:
Mechanosensitive channel MscS solubilized with DDM in open conformation
Method: EM (single particle) / Resolution: 3.1 Å

13006

7oo6

EMDB-13006, PDB-7oo6:
Mechanosensitive channel MscS solubilized with DDM in closed conformation with added lipid
Method: EM (single particle) / Resolution: 3.1 Å

13007

7oo8

EMDB-13007, PDB-7oo8:
Mechanosensitive channel MscS solubilized with LMNG in closed conformation with added lipid
Method: EM (single particle) / Resolution: 3.7 Å

13008

7ooa

EMDB-13008, PDB-7ooa:
Mechanosensitive channel MscS solubilized with LMNG in open conformation with added lipid
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-AV0:
Lauryl Maltose Neopentyl Glycol

ChemComp-HOH:
WATER / Water

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

Source
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli se11 (bacteria)
  • Escherichia coli SE11
KeywordsMEMBRANE PROTEIN / mechanosensitive channel / LMNG stack / delipidation / DDM / LMNG

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