AI Article Synopsis
- Membrane remodeling and repair are crucial processes for all types of cells, involving specific proteins like Vipp1/IM30 in plants, PspA in bacteria, and ESCRT-III in eukaryotes.
- * Recent research indicates that these protein families are evolutionarily related and share a common ancestor that existed before the last universal common ancestor.
- * Structural analyses, including cryo-electron microscopy, reveal that Vipp1 proteins form flexible, dome-shaped rings that can bind and reshape membranes, highlighting the conserved mechanisms of membrane remodeling across different life forms.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8281802 | PMC |
| http://dx.doi.org/10.1016/j.cell.2021.05.041 | DOI Listing |
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Article Synopsis
- Membrane remodeling and repair are crucial processes for all types of cells, involving specific proteins like Vipp1/IM30 in plants, PspA in bacteria, and ESCRT-III in eukaryotes.
- * Recent research indicates that these protein families are evolutionarily related and share a common ancestor that existed before the last universal common ancestor.
- * Structural analyses, including cryo-electron microscopy, reveal that Vipp1 proteins form flexible, dome-shaped rings that can bind and reshape membranes, highlighting the conserved mechanisms of membrane remodeling across different life forms.
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