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Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery
Open accessPublished version of a preprint
Abstract
Most prokaryotes divide using filaments of the tubulin-like FtsZ protein, while some archaea employ instead ESCRT-III-like proteins and their filaments for cell division and cytokinesis. The alternative archaeal system comprises Cdv proteins and is thought to bear some resemblance to ESCRT-III-based membrane remodeling in other domains of life, including eukaryotes, especially during abscission. Here, we present biochemical, crystallographic, and cryo-EM studies of the Sulfolobus Cdv machinery. CdvA, an early non-ESCRT component, adopts a PRC‐domain/coiled-coil fold and polymerizes into long double-stranded helical filaments, mainly via hydrophobic interfaces. Monomeric CdvB adopts the canonical ESCRT-III fold in both a closed and a distinct “semiopen” conformation. Soluble CdvB2 filaments are composed of subunits in the closed state, appearing to transition to the open, active state only when polymerized on membranes. Short N-terminal amphipathic helices in all CdvB paralogues, B, B1, and B2, mediate membrane binding and are required for liposome recruitment in vitro. We provide a molecular overview of archaeal ESCRT-III-based cytokinesis machinery, the definitive demonstration that CdvB proteins are bona fide ESCRT-III homologues, and reveal the molecular basis for membrane engagement. Thus, we illuminate conserved principles of ESCRT-mediated membrane remodeling and extend them to an anciently diverged archaeal lineage.
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Research works printed but not linked: 64
- 10.1038/nrm1745 · DOI
- 10.1016/j.tim.2022.01.005 · DOI
- 10.1038/ncb2482 · DOI
- 10.1016/j.devcel.2014.11.006 · DOI
- 10.1073/pnas.0809467105 · DOI
- 10.1126/science.1165322 · DOI
- 10.1111/mmi.13716 · DOI
- 10.1016/j.molcel.2010.12.018 · DOI
- 10.1126/science.aaz2532 · DOI
- 10.1126/sciadv.ade5224 · DOI
- 10.1146/annurev-cellbio-111822-120242 · DOI
- 10.1073/pnas.2513939122 · DOI
- 10.1093/nar/gkv332 · DOI
- 10.1093/nar/gkab1061 · DOI · Paper page
- 10.1371/journal.pone.0021921 · DOI
- 10.1016/j.jmb.2008.03.030 · DOI
- 10.1038/nsmb.1621 · DOI
- 10.1111/j.1600-0854.2007.00584.x · DOI
- 10.1038/s41594-022-00867-8 · DOI
- 10.1126/science.aad8305 · DOI
- 10.1128/mBio.00417-20 · DOI
- 10.1016/j.jmb.2013.09.043 · DOI
- 10.1038/ncomms9781 · DOI
- 10.1126/sciadv.aba4897 · DOI
- 10.1093/bioinformatics/btn392 · DOI
- 10.1093/bib/bbx108 · DOI · Paper page
- 10.1016/j.bbalip.2016.12.006 · DOI
- 10.1074/jbc.M111.283671 · DOI
- 10.1016/j.devcel.2013.09.009 · DOI
- 10.1038/s41592-022-01488-1 · DOI · Paper page
- 10.1126/sciadv.ads5255 · DOI · Paper page
- 10.1016/j.jsb.2022.107897 · DOI
- N. D. Franceschi, A. Blanch-Jover, C. Dekker, Interaction hierarchy among Cdv proteins drives recruitment to membrane necks. eLife 14, RP104226 (2025).
- 10.1091/mbc.e12-11-0785 · DOI
- 10.1126/science.1203285 · DOI
- 10.1016/j.cell.2021.05.041 · DOI
- 10.1073/pnas.2319115121 · DOI
- 10.1083/jcb.201403108 · DOI
- 10.1016/j.tcb.2021.04.005 · DOI
- 10.1038/s41594-020-0404-x · DOI
- 10.1016/j.febslet.2009.10.022 · DOI
- 10.1016/j.jmb.2013.12.016 · DOI
- 10.1016/j.bbamem.2016.10.018 · DOI
- 10.1038/s41594-024-01399-z · DOI
- 10.1016/j.cell.2021.05.011 · DOI
- 10.1038/s44318-024-00346-4 · DOI
- 10.1128/AEM.01608-13 · DOI
- 10.1007/BF00408082 · DOI
- 10.1016/S0969-2126(00)80052-0 · DOI
- 10.1006/jmbi.1993.1012 · DOI
- 10.1016/j.pbiomolbio.2004.07.009 · DOI
- 10.1016/j.jsb.2017.02.003 · DOI
- 10.7554/eLife.42166 · DOI
- 10.1042/BCJ20210708 · DOI
- 10.1002/pro.3943 · DOI
- 10.1038/s41586-024-07215-4 · DOI · Paper page
- 10.1107/S0907444910007493 · DOI · Paper page
- 10.1107/S2059798318002425 · DOI
- 10.1107/S2059798319011471 · DOI · Paper page
- 10.1002/1873-3468.13471 · DOI
- S. V. Albers, W. N. Konings, A. J. Driessen, “Chapter 7: Membranes of thermophiles and other extremophiles” in Methods in Microbiology, F. A. Rainey, A. Ore, Eds. (Academic Press, 2006), pp. 161–171.
- 10.1006/jsbi.1999.4155 · DOI
- 10.1038/s41592-019-0575-8 · DOI
- 10.1039/D2FD00034B · DOI
Metadata
- Authors
- Drobnič, T., Salzer, R., Nierhaus, T., Jiang, M. K. X., Bellini, D., Steindorf, A., Albers, S.-V., Baum, B., & Löwe, J.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Freiburg (DE)
- Corresponding author
- Löwe, Jan
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2026-01-16
- Volume
- 123
- Issue
- 3
- Pages
- e2525941123-e2525941123
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC12818579
- OpenAlex
- W7124448602
- Cited by
- 5
- References
- 2
- Citations by year
- 2026: 5
- FWCI
- 16.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Funders
- UKRI | Medical Research Council (U105184326)
- UK Research and Innovation (MC_UP_1201/27)
- Wellcome Trust (227876/Z/23/Z, 203276/Z/16/Z, 222460/Z/21/Z)
- Volkswagen Foundation (94933)
- Deutsche Forschungsgemeinschaft (390939984)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- ESCRT-III, archaeal cell division, Sulfolobus, cytokinesis, membrane remodeling, coiled coil, amphipathic helix, membrane binding, protein polymerization, abscission
- MeSH terms
- Cell Division, Models, Molecular, Sulfolobus, Crystallography, X-Ray, Archaeal Proteins, Cryoelectron Microscopy, Cytokinesis, Endosomal Sorting Complexes Required for Transport
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