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

Publication type:
Journal article
Metadata:
Autoren
  • Benedikt Junglas
  • Stefan T Huber
  • Thomas Heidler
  • Lukas Schlösser
  • Daniel Mann
  • Raoul Hennig
  • Mairi Clarke
  • Nadja Hellmann
  • Dirk Schneider
  • Carsten Sachse
DOI
10.1016/j.cell.2021.05.042
ISSN
0092-8674
Ausgabe der Veröffentlichung
14
Zeitschrift
Cell
Sprache
en
Paginierung
3674 - 3688.e18
Datum der Veröffentlichung
2021
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.cell.2021.05.042
Datum der Datenerfassung
2023
Titel
PspA adopts an ESCRT-III-like fold and remodels bacterial membranes
Ausgabe der Zeitschrift
184

Data source: Crossref

Other metadata sources:
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.
Addresses
  • Ernst-Ruska Centre for Microscopy and Spectroscopy with Electrons, ER-C-3/Structural Biology, Forschungszentrum Jülich, 52425 Jülich, Germany; JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, 52425 Jülich, Germany; Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
Autoren
  • Benedikt Junglas
  • Stefan T Huber
  • Thomas Heidler
  • Lukas Schlösser
  • Daniel Mann
  • Raoul Hennig
  • Mairi Clarke
  • Nadja Hellmann
  • Dirk Schneider
  • Carsten Sachse
DOI
10.1016/j.cell.2021.05.042
eISSN
1097-4172
Externe Identifier
  • PubMed Identifier: 34166616
Open access
false
ISSN
0092-8674
Ausgabe der Veröffentlichung
14
Zeitschrift
Cell
Schlüsselwörter
  • Cell Membrane
  • Escherichia coli
  • Lipid Bilayers
  • Bacterial Proteins
  • Heat-Shock Proteins
  • Cryoelectron Microscopy
  • Endocytosis
  • Amino Acid Sequence
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Models, Molecular
  • Unilamellar Liposomes
  • Endosomal Sorting Complexes Required for Transport
  • Protein Domains
Sprache
eng
Medium
Print-Electronic
Online publication date
2021
Paginierung
3674 - 3688.e18
Datum der Veröffentlichung
2021
Status
Published
Datum der Datenerfassung
2021
Titel
PspA adopts an ESCRT-III-like fold and remodels bacterial membranes.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
184

Data source: Europe PubMed Central

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.
Date of acceptance
2021
Autoren
  • Benedikt Junglas
  • Stefan T Huber
  • Thomas Heidler
  • Lukas Schlösser
  • Daniel Mann
  • Raoul Hennig
  • Mairi Clarke
  • Nadja Hellmann
  • Dirk Schneider
  • Carsten Sachse
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/34166616
DOI
10.1016/j.cell.2021.05.042
eISSN
1097-4172
Ausgabe der Veröffentlichung
14
Zeitschrift
Cell
Schlüsselwörter
  • ESCRT-III
  • IM30
  • PspA
  • Vipp1
  • cryo-EM
  • cryo-ET
  • helical reconstruction
  • membrane fission
  • membrane fusion
  • membrane remodeling
  • membrane tubulation
  • Amino Acid Sequence
  • Bacterial Proteins
  • Cell Membrane
  • Cryoelectron Microscopy
  • Endocytosis
  • Endosomal Sorting Complexes Required for Transport
  • Escherichia coli
  • Heat-Shock Proteins
  • Lipid Bilayers
  • Models, Molecular
  • Protein Domains
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Unilamellar Liposomes
Sprache
eng
Country
United States
Paginierung
3674 - 3688.e18
PII
S0092-8674(21)00697-8
Datum der Veröffentlichung
2021
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2022
Titel
PspA adopts an ESCRT-III-like fold and remodels bacterial membranes.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
184

Data source: PubMed

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