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

Autor:	Liu J; Department of Infectious Disease, Imperial College, London, UK., Tassinari M; Department of Infectious Disease, Imperial College, London, UK., Souza DP; MRC Laboratory for Molecular Cell Biology, University College London, London, UK; Division of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, UK., Naskar S; Department of Infectious Disease, Imperial College, London, UK., Noel JK; Max Delbrück Center for Molecular Medicine, Berlin, Germany., Bohuszewicz O; Department of Infectious Disease, Imperial College, London, UK., Buck M; Department of Life Sciences, Imperial College, London, UK., Williams TA; School of Biological Sciences, University of Bristol, Bristol, UK., Baum B; MRC Laboratory for Molecular Cell Biology, University College London, London, UK; Division of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, UK; Institute for the Physics of Living Systems, University College London, London, UK. Electronic address: bbaum@mrc-lmb.cam.ac.uk., Low HH; Department of Infectious Disease, Imperial College, London, UK. Electronic address: h.low@imperial.ac.uk.
Jazyk:	angličtina
Zdroj:	Cell [Cell] 2021 Jul 08; Vol. 184 (14), pp. 3660-3673.e18. Date of Electronic Publication: 2021 Jun 23.
DOI:	10.1016/j.cell.2021.05.041
Abstrakt:	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. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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