PspA adopts an ESCRT-III-like fold and remodels bacterial membranes

PspA is the main effector of the phage shock protein (Psp) system and preserves the bacterial inner membrane integrity and function. Here, we present the 3.6 Å resolution cryoelectron microscopy (cryo-EM) structure of PspA assembled in helical rods. PspA monomers adopt a canonical ESCRT-III fold in...

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Veröffentlicht in:Cell Jg. 184; H. 14; S. 3674
Hauptverfasser: Junglas, Benedikt, Huber, Stefan T, Heidler, Thomas, Schlösser, Lukas, Mann, Daniel, Hennig, Raoul, Clarke, Mairi, Hellmann, Nadja, Schneider, Dirk, Sachse, Carsten
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 08.07.2021
Schlagworte:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bacterial Proteins - ultrastructure
Cell Membrane - metabolism
Cryoelectron Microscopy
Endocytosis
Endosomal Sorting Complexes Required for Transport - chemistry
Endosomal Sorting Complexes Required for Transport - metabolism
Escherichia coli - metabolism
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Heat-Shock Proteins - ultrastructure
Lipid Bilayers - metabolism
Models, Molecular
Protein Domains
Protein Structure, Secondary
Sequence Homology, Amino Acid
Unilamellar Liposomes - metabolism
helical reconstruction
PspA
IM30
Vipp1
membrane remodeling
ESCRT-III
membrane fission
membrane tubulation
cryo-ET
cryo-EM
membrane fusion
ISSN:1097-4172, 1097-4172
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Zusammenfassung:PspA is the main effector of the phage shock protein (Psp) system and preserves the bacterial inner membrane integrity and function. Here, we present the 3.6 Å resolution cryoelectron microscopy (cryo-EM) structure of PspA assembled in helical rods. PspA monomers adopt a canonical ESCRT-III fold in an extended open conformation. PspA rods are capable of enclosing lipids and generating positive membrane curvature. Using cryo-EM, we visualized how PspA remodels membrane vesicles into μm-sized structures and how it mediates the formation of internalized vesicular structures. Hotspots of these activities are zones derived from PspA assemblies, serving as lipid transfer platforms and linking previously separated lipid structures. These membrane fusion and fission activities are in line with the described functional properties of bacterial PspA/IM30/LiaH proteins. Our structural and functional analyses reveal that bacterial PspA belongs to the evolutionary ancestry of ESCRT-III proteins involved in membrane remodeling.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1097-4172
1097-4172
DOI:10.1016/j.cell.2021.05.042