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-Structure paper
タイトル | Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily. |
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ジャーナル・号・ページ | Cell, Vol. 184, Issue 14, Page 3660-3673.e18, Year 2021 |
掲載日 | 2021年7月8日 |
著者 | Jiwei Liu / Matteo Tassinari / Diorge P Souza / Souvik Naskar / Jeffrey K Noel / Olga Bohuszewicz / Martin Buck / Tom A Williams / Buzz Baum / Harry H Low / |
PubMed 要旨 | 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, ...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. |
リンク | Cell / PubMed:34166615 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 6.5 - 9.4 Å |
構造データ | EMDB-11468, PDB-6zvr: EMDB-11469, PDB-6zvs: EMDB-11470, PDB-6zvt: EMDB-11478, PDB-6zw4: EMDB-11481, PDB-6zw5: EMDB-11482, PDB-6zw6: EMDB-11483, PDB-6zw7: |
由来 |
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キーワード | LIPID BINDING PROTEIN / membrane remodelling |