Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodelling superfamily
| Autor: | Martin Buck, Souvik Naskar, Buzz Baum, Jeffrey K. Noel, Jiwei Liu, Matteo Tassinari, Diorge P. Souza, Tom A. Williams, Harry H. Low, Olga Bohuszewicz |
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| Přispěvatelé: | Wellcome Trust |
| Rok vydání: | 2021 |
| Předmět: |
Cancer Research
Biochemistry & Molecular Biology PLASTIDS 1 ESCRT-III STRESS Protein family SYNECHOCYSTIS LUCA PspA CELL-DIVISION cryoelectron microscopy macromolecular substances ORGANIZATION Biology General Biochemistry Genetics and Molecular Biology ESCRT Homology (biology) Article 03 medical and health sciences 0302 clinical medicine PHAGE-SHOCK-PROTEIN Three-domain system REVEALS evolution Plastid Cytoskeleton 11 Medical and Health Sciences 030304 developmental biology 0303 health sciences Science & Technology COMPLEX VESICLE-INDUCING PROTEIN Last universal ancestor cytoskeleton Cell Biology eukaryogenesis 06 Biological Sciences Cell biology Membrane Vipp1/IM30 membrane remodeling ring structure Life Sciences & Biomedicine 030217 neurology & neurosurgery SYSTEM Developmental Biology |
| Zdroj: | 3673.e18 Cell Liu, J, Tassinari, M, Souza, D, Naskar, S, Noel, J K, Bohuszewicz, O, Buck, M, Williams, T, Baum, B & Low, H H 2021, ' Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily ', Cell, vol. 184, no. 14, pp. 3660-3673.e18 . https://doi.org/10.1016/j.cell.2021.05.041 |
| DOI: | 10.1016/j.cell.2021.05.041 |
| Popis: | Summary 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. Graphical abstract Highlights • PspA, Vipp1, and ESCRT-III are members of the same polymer-forming protein family • ESCRT-III-like polymers function to remodel membranes across all domains of life • Hinges in the Vipp1 monomer enable it to form a diverse set of flexible polymers • The inner lumen of the dome-shaped Vipp1 ring binds and deforms membranes Phylogenetic and structural characterization of Vipp1 and PspA identifies them as ESCRT-III homologs and part of an ancient family of protein polymers that remodel membranes across the domains of life. |
| Databáze: | OpenAIRE |
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