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Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily

DOI: 10.1016/j.cell.2021.05.041 DOI Help

Authors: Jiwei Liu (Imperial College, London) , Matteo Tassinari (Imperial College, Londo) , Diorge P. De Souza (MRC Laboratory of Molecular Biology; University College London) , Souvik Naskar (Imperial College, London) , Jeffrey K. Noel (Max Delbrück Center for Molecular Medicine) , Olga Bohuszewicz (Imperial College, London) , Martin Buck (Imperial College, London) , Tom A. Williams (University of Bristol) , Buzz Baum (University College London; MRC Laboratory of Molecular Biology) , Harry H. Low (Imperial College, London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell , VOL 184 , PAGES 3660 - 3673.e18

State: Published (Approved)
Published: July 2021
Diamond Proposal Number(s): 16942

Open Access Open Access

Abstract: Membrane remodeling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, and ESCRT-III in eukaryotes. Here, using a combination of evolutionary and structural analyses, we show that these protein families are homologous and share a common ancient evolutionary origin that likely predates the last universal common ancestor. This homology is evident in cryo-electron microscopy structures of Vipp1 rings from the cyanobacterium Nostoc punctiforme presented over a range of symmetries. Each ring is assembled from rungs that stack and progressively tilt to form dome-shaped curvature. Assembly is facilitated by hinges in the Vipp1 monomer, similar to those in ESCRT-III proteins, which allow the formation of flexible polymers. Rings have an inner lumen that is able to bind and deform membranes. Collectively, these data suggest conserved mechanistic principles that underlie Vipp1, PspA, and ESCRT-III-dependent membrane remodeling across all domains of life.

Journal Keywords: pp1/IM30; PspA; ESCRT-III; membrane remodeling; cryoelectron microscopy; ring structure; cytoskeleton; LUCA; evolution; eukaryogenesis

Diamond Keywords: Cyanobacteria

Subject Areas: Biology and Bio-materials, Chemistry

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

Added On: 22/07/2021 09:44

Discipline Tags:

Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Microscopy Electron Microscopy (EM) Cryo Electron Microscopy (Cryo EM)