ArticleThe Journal of cell biology2022
Filament organization of the bacterial actin MreB is dependent on the nucleotide state.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Proteomic Evidence for Biofilm-Mediated Copper Stress Adaptation in Oleidesulfovibrio alaskensis G20.Environmental microbiology · 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
- Mutational analysis of the F plasmid partitioning protein ParA reveals residues required for oligomerization and plasmid maintenance.Nucleic acids research · 2025Article
- Improving Stability ofBio-protocol · 2024Article
- Article
- Developing a new host-vector system forFrontiers in microbiology · 2024Article
- Getting bacterial cells into shape.eLife · 2023Article
- Article
- Assembly properties of bacterial actin MreB involved in Spiroplasma swimming motility.The Journal of biological chemistry · 2023Article
- A mechanism of salt bridge-mediated resistance to FtsZ inhibitor PC190723 revealed by a cell-based screen.Molecular biology of the cell · 2023Article
- Purification and ATPase Activity Measurement of Spiroplasma MreB.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Solubility and Thermal Stability ofInternational journal of molecular sciences · 2022Article
- Cytoskeletal components can turn wall-less spherical bacteria into kinking helices.Nature communications · 2022Article
- Characterization of heterologously expressed Fibril, a shape and motility determining cytoskeletal protein of the helical bacteriumiScience · 2022Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
MreB, the bacterial ancestor of eukaryotic actin, is responsible for shape in most rod-shaped bacteria. Despite belonging to the actin family, the relevance of nucleotide-driven polymerization dynamics for MreB function is unclear. Here, we provide insights into the effect of nucleotide state on membrane binding of Spiroplasma citri MreB5 (ScMreB5). Filaments of ScMreB5WT and an ATPase-deficient mutant, ScMreB5E134A, assemble independently of the nucleotide state. However, capture of the filament dynamics revealed that efficient filament formation and organization through lateral interactions are affected in ScMreB5E134A. Hence, the catalytic glutamate functions as a switch, (a) by sensing the ATP-bound state for filament assembly and (b) by assisting hydrolysis, thereby potentially triggering disassembly, as observed in other actins. Glu134 mutation and the bound nucleotide exhibit an allosteric effect on membrane binding, as observed from the differential liposome binding. We suggest that the conserved ATP-dependent polymerization and disassembly upon ATP hydrolysis among actins has been repurposed in MreBs for modulating filament organization on the membrane.
Indexed as
Identifiers
What OpenQuestion holds
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.