PspA adopts an ESCRT-III-like fold and remodels bacterial membranes.
Cell
; 184(14): 3674-3688.e18, 2021 07 08.
Article
en En
| MEDLINE
| ID: mdl-34166616
ABSTRACT
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Membrana Celular
/
Complejos de Clasificación Endosomal Requeridos para el Transporte
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Proteínas de Choque Térmico
Idioma:
En
Revista:
Cell
Año:
2021
Tipo del documento:
Article