ArticleThe Journal of biological chemistry2023
Assembly properties of bacterial actin MreB involved in Spiroplasma swimming motility.
Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Multilevel Regulation of Peptidoglycan Dynamics in Bacteria: From Molecular Mechanisms to Applied Perspectives.Biomolecules · 2026Review
- Live imaging of bacterial actin MreBs fromBiophysics and physicobiology · 2026Article
- Cooperative and divergent properties of bacterial actin isoforms inBiophysics and physicobiology · 2026Article
- MreB: unraveling the molecular mechanisms of bacterial shape, division, and environmental adaptation.Cell communication and signaling : CCS · 2025Review
- Deciphering the impact of MreB on the morphology and pathogenicity of the aquatic pathogen Spiroplasma eriocheiris.Biology direct · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial actin MreB forms filaments composed of antiparallel double-stranded units. The wall-less helical bacterium Spiroplasma has five MreB homologs (MreB1-5), some of which are involved in an intracellular ribbon for driving the bacterium's swimming motility. Although the interaction between MreB units is important for understanding Spiroplasma swimming, the interaction modes of each ribbon component are unclear. Here, we examined the assembly properties of Spiroplasma eriocheiris MreB5 (SpeMreB5), one of the ribbon component proteins that forms sheets. Electron microscopy revealed that sheet formation was inhibited under acidic conditions and bundle structures were formed under acidic and neutral conditions with low ionic strength. We also used solution assays and identified four properties of SpeMreB5 bundles as follows: (I) bundle formation followed sheet formation; (II) electrostatic interactions were required for bundle formation; (III) the positively charged and unstructured C-terminal region contributed to promoting lateral interactions for bundle formation; and (IV) bundle formation required Mg
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Registered trials
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