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Salactin, a dynamically unstable actin homolog in Haloarchaea
Open accessPreprint — published as 10.1128/mbio.02272-23 · Paper page
Abstract
Across the domains of life, actin homologs are integral components of many essential processes such as DNA segregation, cell division, and cell shape determination. Archaea genomes, like those of bacteria and eukaryotes, also encode actin homologs, but much less is known about these proteins’ in vivo dynamics and cellular functions. We identified and characterized the function and dynamics of Salactin, an actin homolog in the hypersaline archaeon Halobacterium salinarum. Despite Salactin’s homology to bacterial MreB proteins, we find it does not function as a MreB ortholog in H. salinarum. Rather, live-cell imaging revealed that Salactin forms dynamically unstable filaments that grow and shrink out of the cell poles. Like other dynamically unstable polymers, Salactin monomers add at the growing filament end and its ATP-bound critical concentration is substantially lower than the ADP-bound form. When H. salinarum’s chromosomal copy number becomes limiting under low phosphate growth conditions, cells lacking Salactin show perturbed DNA distributions. Taken together, we propose that Salactin is part of a previously unknown chromosomal segregation apparatus required during low-ploidy conditions.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Zheng, J., Lammers, A., Mallon, J., Litschel, T., Moody, E. R. R., Ramirez-Diaz, D. A., Schmid, A., Williams, T. A., Bisson-Filho, A. W., & Garner, E.
- Affiliations
- Harvard University (US)
- Boston University (US)
- Brandeis University (US)
- Marine Biological Laboratory (US)
- University of Bristol (GB)
- Duke University (US)
- Corresponding author
- Garner, Ethan
- ORCID
- Venue
- mBio
- Publisher
- openRxiv
- Published
- 2023-03-10
- Volume
- 14
- Issue
- 6
- Pages
- e0227223-e0227223
- ISSN
- 2150-7511 (ISSN-L)
- PMC
- PMC10746226
- OpenAlex
- W4388698053
- Cited by
- 8
- References
- 1
- Citations by year
- 2025: 4 · 2024: 4
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- mBio (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open Access Server of the Woods Hole Scientific Community (Woods Hole Scientific Community) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Explore Bristol Research (submittedVersion, cc-by)
- Bristol Research (University of Bristol) (submittedVersion, cc-by)
- Funders
- National Science Foundation (2011846, 1651117, 2222076, CAREER, 1764269)
- Pew Charitable Trusts
- Simons Foundation (GR404060)
- John Templeton Foundation (62220)
- Gordon and Betty Moore Foundation (GBMF9741, 62220)
- Harvard University (1764269)
- Wellcome Trust (203276/l/16/Z)
- Materials Research Science and Engineering Center, Harvard University (DMR-2011846, 2011846)
- Division of Materials Research (DMR-2011846, 2011846)
- 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 Mechanics and Interactions
- Keywords
- actin homolog, Halobacterium salinarum, halophilic archaea, dynamic instability, filament polymerization, DNA segregation, chromosomal copy number, cell division
- MeSH terms
- Actins, Archaeal Proteins
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