ArticleProceedings of the National Academy of Sciences of the United States of America2014
Effects of polymerization and nucleotide identity on the conformational dynamics of the bacterial actin homolog MreB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- Alanine-scanning mutagenesis library of MreB reveals distinct roles for regulating cell shape and viability.PLoS genetics · 2026Article
- Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 2024Article
- Article
- Solubility and Thermal Stability ofInternational journal of molecular sciences · 2022Article
- Enzyme 1 of the phosphoenolpyruvate:sugar phosphotransferase system is involved in resistance to MreB disruption in wild-type and ∆envC cells.Molecular microbiology · 2022Article
- Filament organization of the bacterial actin MreB is dependent on the nucleotide state.The Journal of cell biology · 2022Article
- Multiple conserved states characterize the twist landscape of the bacterial actin homolog MreB.Computational and structural biotechnology journal · 2022Article
- AimB Is a Small Protein Regulator of Cell Size and MreB Assembly.Biophysical journal · 2020Article
- Intracellular ion concentrations and cation-dependent remodelling of bacterial MreB assemblies.Scientific reports · 2020Article
- Chiral twisting in a bacterial cytoskeletal polymer affects filament size and orientation.Nature communications · 2020Article
- Conservation of conformational dynamics across prokaryotic actins.PLoS computational biology · 2019Article
- Status of Targeting MreB for the Development of Antibiotics.Frontiers in chemistry · 2019Review
- MreB polymers and curvature localization are enhanced by RodZ and predict E. coli's cylindrical uniformity.Nature communications · 2018Article
- RodZ modulates geometric localization of the bacterial actin MreB to regulate cell shape.Nature communications · 2018Article
- Review
- Shape Selection of Surface-Bound Helical Filaments: Biopolymers on Curved Membranes.Biophysical journal · 2016Article
- MreB Orientation Correlates with Cell Diameter in Escherichia coli.Biophysical journal · 2016Article
- YodL and YisK Possess Shape-Modifying Activities That Are Suppressed by Mutations in Bacillus subtilis mreB and mbl.Journal of bacteriology · 2016Article
- Bacterial actin and tubulin homologs in cell growth and division.Current biology : CB · 2015Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The assembly of protein filaments drives many cellular processes, from nucleoid segregation, growth, and division in single cells to muscle contraction in animals. In eukaryotes, shape and motility are regulated through cycles of polymerization and depolymerization of actin cytoskeletal networks. In bacteria, the actin homolog MreB forms filaments that coordinate the cell-wall synthesis machinery to regulate rod-shaped growth and contribute to cellular stiffness through unknown mechanisms. Like actin, MreB is an ATPase and requires ATP to polymerize, and polymerization promotes nucleotide hydrolysis. However, it is unclear whether other similarities exist between MreB and actin because the two proteins share low sequence identity and have distinct cellular roles. Here, we use all-atom molecular dynamics simulations to reveal surprising parallels between MreB and actin structural dynamics. We observe that MreB exhibits actin-like polymerization-dependent structural changes, wherein polymerization induces flattening of MreB subunits, which restructures the nucleotide-binding pocket to favor hydrolysis. MreB filaments exhibited nucleotide-dependent intersubunit bending, with hydrolyzed polymers favoring a straighter conformation. We use steered simulations to demonstrate a coupling between intersubunit bending and the degree of flattening of each subunit, suggesting cooperative bending along a filament. Taken together, our results provide molecular-scale insight into the diversity of structural states of MreB and the relationships among polymerization, hydrolysis, and filament properties, which may be applicable to other members of the broad actin family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.