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Cited by 12Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationMicrotubule and mitosis dynamics

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MreB: unraveling the molecular mechanisms of bacterial shape, division, and environmental adaptation

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Wang, Yaqi, jiang, Yalan, Song, Zhixuan, Zhu, Chengbin, Tang, Yujun, Peng, Jiaofeng, Liu, Peng·2025·Cell Communication and Signaling
DOI 10.1186/s12964-025-02373-yPMC PMC12372405
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Abstract

As a key bacterial actin-like protein, MreB plays crucial roles in maintaining cell shape, regulating peptidoglycan synthesis, and coordinating chromosome segregation, making it a promising target for novel antibiotics. This review comprehensively explores MreB’s molecular architecture, its assembly into antiparallel protofilaments, and its pivotal roles in bacterial cell morphology and division. We also delve into how MreB interacts with membrane-associated proteins such as RodZ and MreC/D to coordinate cell wall synthesis and respond to environmental signals like ion gradients and temperature changes. Furthermore, we highlight the cooperation and functional divergence between MreB and FtsZ, underscoring the evolutionary adaptability of bacterial cytoskeletal structures. The structural and functional parallels between MreB and eukaryotic cytoskeletal proteins are also examined, offering new insights into the evolution of cytoskeletal systems. By integrating insights from structural biology, synthetic biology, and microbial ecology, this review aims to provide a deeper understanding of MreB’s role in bacterial biology, its dynamic responses to environmental cues, and its implications for therapeutic innovation. This comprehensive analysis not only enhances our knowledge of bacterial self-organization mechanisms but also paves the way for the development of innovative antimicrobial strategies to address the growing challenge of antibiotic resistance.

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Fig. 1 Discovery History and Evolutionary Tree of MreB Protein Functions. A The timeline, progressing from left to right, begins with the emergence of the MreB protein. Subsequent gene duplication events drove the diversification of MreB’s functions. Horizontal gene transfer then enabled MreB to contribute to the development of antibiotic resistance. Ultimately, MreB adapted to cell wall-less environments and evolved the capacity for helical movement. B Maximum-likelihood tree of MreB and MreB-like protein sequences from diverse bacterial species generated using MEGA 11. Branches are color-coded to highlight major functional categories: blue signifies proteins involved in maintaining cell shape; red identifies proteins associated with antibiotic resistance; and green denotes specialized cytoskeletal variants. Bootstrap values ≥ 60% are labeled for major nodes
Fig. 1 Discovery History and Evolutionary Tree of MreB Protein Functions. A The timeline, progressing from left to right, begins with the emergence of the MreB protein. Subsequent gene duplication events drove the diversification of MreB’s functions. Horizontal gene transfer then enabled MreB to contribute to the development of antibiotic resistance. Ultimately, MreB adapted to cell wall-less environments and evolved the capacity for helical movement. B Maximum-likelihood tree of MreB and MreB-like protein sequences from diverse bacterial species generated using MEGA 11. Branches are color-coded to highlight major functional categories: blue signifies proteins involved in maintaining cell shape; red identifies proteins associated with antibiotic resistance; and green denotes specialized cytoskeletal variants. Bootstrap values ≥ 60% are labeled for major nodesCC BY · PubMed Central
Fig. 2 Structural features of MreB and actin. A Predicted secondary structures of MreB orthologs from four key bacterial groups: B. subtilis (Gram-positive), E. coli (Gram-negative), T. maritima (extremophile) and S. citri (wall-less), as generated by ESPrint 3. 0. B Sequence conservation analysis of MreB from the four bacterial groups listed was performed using WebLogo, highlighting the positions of highly conserved amino acid residues. C The domain architecture of B. taurus actin, which includes domains I through IV, is presented for structural comparison with other proteins. D An interaction model between B. taurus actin (blue) and G. stearothermophilus MreB (purple) was generated using AlphaFold3. Regions of significant structural misalignment are highlighted in orange. E The ATP-binding pocket in G. stearothermophilus MreB is visualized using PyMOL, with key residues (T15, A16, N17, G161, G162, T163, E209, K212, G289) labeled
Fig. 2 Structural features of MreB and actin. A Predicted secondary structures of MreB orthologs from four key bacterial groups: B. subtilis (Gram-positive), E. coli (Gram-negative), T. maritima (extremophile) and S. citri (wall-less), as generated by ESPrint 3. 0. B Sequence conservation analysis of MreB from the four bacterial groups listed was performed using WebLogo, highlighting the positions of highly conserved amino acid residues. C The domain architecture of B. taurus actin, which includes domains I through IV, is presented for structural comparison with other proteins. D An interaction model between B. taurus actin (blue) and G. stearothermophilus MreB (purple) was generated using AlphaFold3. Regions of significant structural misalignment are highlighted in orange. E The ATP-binding pocket in G. stearothermophilus MreB is visualized using PyMOL, with key residues (T15, A16, N17, G161, G162, T163, E209, K212, G289) labeledCC BY · PubMed Central
Fig. 3 Structural and functional comparison between MreB and eukaryotic actin. A Eukaryotic Actin System: G-actin monomers polymerize ATP-dependently into polarized double-helical F-actin filaments, undergoing dynamic cycles regulated by ATP hydrolysis. Actin drives cell motility, cytokinesis, vesicle trafficking, and intracellular transport. B Bacterial MreB System: MreB monomers assemble via ATP binding into short, rigid, single-stranded helical filaments. MreB maintains bacterial shape by coordinating peptidoglycan synthesis enzymes during cell wall elongation
Fig. 3 Structural and functional comparison between MreB and eukaryotic actin. A Eukaryotic Actin System: G-actin monomers polymerize ATP-dependently into polarized double-helical F-actin filaments, undergoing dynamic cycles regulated by ATP hydrolysis. Actin drives cell motility, cytokinesis, vesicle trafficking, and intracellular transport. B Bacterial MreB System: MreB monomers assemble via ATP binding into short, rigid, single-stranded helical filaments. MreB maintains bacterial shape by coordinating peptidoglycan synthesis enzymes during cell wall elongationCC BY · PubMed Central
Fig. 4 Integrated description of the MreB/Mbl/MreBH cytoskeletal system. The MreB/Mbl/MreBH cytoskeletal system orchestrates critical bacterial functions through functional redundancy and ATP-dependent dynamic behaviors, enabling multidimensional regulation. Central to cell morphogenesis, this system coordinates helical peptidoglycan synthesis and interacts with RodZ; its triple deletion (MreB/Mbl/MreBH) disrupts cell shape maintenance, leading to spherical morphology and lysis. Concurrently, it regulates chromosome segregation by positioning the SMC complex, ensuring bidirectional origin localization during replication, and exhibiting compatibility with heterologous expression systems. Environmental adaptability is mediated via stress-responsive mechanisms, including suppressor mutations such as som-1, and growth rate modulation under adverse conditions. Dynamic ATP-driven filament extension/contraction underpins its mechanical plasticity, validated by FRAP-based subunit exchange assays. Targeted regulation is achieved through dedicated pathways, such as YodL regulating MreB and YisK regulating Mbl, highlighting its integration into broader cellular networks
Fig. 4 Integrated description of the MreB/Mbl/MreBH cytoskeletal system. The MreB/Mbl/MreBH cytoskeletal system orchestrates critical bacterial functions through functional redundancy and ATP-dependent dynamic behaviors, enabling multidimensional regulation. Central to cell morphogenesis, this system coordinates helical peptidoglycan synthesis and interacts with RodZ; its triple deletion (MreB/Mbl/MreBH) disrupts cell shape maintenance, leading to spherical morphology and lysis. Concurrently, it regulates chromosome segregation by positioning the SMC complex, ensuring bidirectional origin localization during replication, and exhibiting compatibility with heterologous expression systems. Environmental adaptability is mediated via stress-responsive mechanisms, including suppressor mutations such as som-1, and growth rate modulation under adverse conditions. Dynamic ATP-driven filament extension/contraction underpins its mechanical plasticity, validated by FRAP-based subunit exchange assays. Targeted regulation is achieved through dedicated pathways, such as YodL regulating MreB and YisK regulating Mbl, highlighting its integration into broader cellular networksCC BY · PubMed Central
Fig. 5 The fundamental mechanism underlying bacterial cell wall synthesis and morphological maintenance involves the interaction and function of key proteins. Green (PspA): A membrane protein regulating mechanical stress via interactions with RodZ and MreB. Red (MreB): A cytoskeletal protein coordinating cell wall synthesis, division site localization, and morphological homeostasis, collaborating with FtsZ. Dark Blue (RodZ): The main regulatory factor for MreB, connecting MreB with cell wall synthetases. Pink (FtsZ): A splitting ring protein driving division ring contraction, relying on MreB for cell wall remodeling. Orange (RodA): A peptidoglycan synthetase inserting and extending peptidoglycan chains, regulated by MreB and RodZ. Purple (MurG): A peptidoglycan precursor synthetase working with MreD. Blue (PBP2): Penicillin-binding proteins in cell wall synthesis, regulated by MreC. Yellow (CbtA): A toxin disrupting membrane pressure sensing and PspA function. Light Gray (FtsZ ring): The division ring facilitating contractile processes. Gray (MreC-MreD complex): A complex organizing peptidoglycan synthetases and regulating precursor synthesis
Fig. 5 The fundamental mechanism underlying bacterial cell wall synthesis and morphological maintenance involves the interaction and function of key proteins. Green (PspA): A membrane protein regulating mechanical stress via interactions with RodZ and MreB. Red (MreB): A cytoskeletal protein coordinating cell wall synthesis, division site localization, and morphological homeostasis, collaborating with FtsZ. Dark Blue (RodZ): The main regulatory factor for MreB, connecting MreB with cell wall synthetases. Pink (FtsZ): A splitting ring protein driving division ring contraction, relying on MreB for cell wall remodeling. Orange (RodA): A peptidoglycan synthetase inserting and extending peptidoglycan chains, regulated by MreB and RodZ. Purple (MurG): A peptidoglycan precursor synthetase working with MreD. Blue (PBP2): Penicillin-binding proteins in cell wall synthesis, regulated by MreC. Yellow (CbtA): A toxin disrupting membrane pressure sensing and PspA function. Light Gray (FtsZ ring): The division ring facilitating contractile processes. Gray (MreC-MreD complex): A complex organizing peptidoglycan synthetases and regulating precursor synthesisCC BY · PubMed Central
Fig. 6 Dynamic regulation network of MreB polymerization and species heterogeneity. MreB polymerization is regulated through temperature-dependent feedback mechanisms, such as the reduction of critical concentration at high temperatures by T. maritima to facilitate stable assembly. It is also influenced by ionic gradient modulation, where monovalent ions inhibit nucleation while divalent ions promote elongation, with ion concentrations determining the microstructure morphology. Additionally, MreB polymerization involves coupling with nucleotide metabolism: ATP and GTP drive the initiation process, ADP helps maintain equilibrium, and the type of nucleotide dictates structural transitions. Different species exhibit heterogeneity: Bacillus depends on high divalent ion concentrations and pH sensitivity, S. pneumoniae forms pH-Mg²⁺-dependent lateral interactions via its positively charged C-terminal domain, and T. maritima relies on nucleotide cycling for low critical concentration adaptation across temperatures. These findings highlight the evolutionary plasticity and environmentally adaptive molecular design in prokaryotic morphogenesis networks
Fig. 6 Dynamic regulation network of MreB polymerization and species heterogeneity. MreB polymerization is regulated through temperature-dependent feedback mechanisms, such as the reduction of critical concentration at high temperatures by T. maritima to facilitate stable assembly. It is also influenced by ionic gradient modulation, where monovalent ions inhibit nucleation while divalent ions promote elongation, with ion concentrations determining the microstructure morphology. Additionally, MreB polymerization involves coupling with nucleotide metabolism: ATP and GTP drive the initiation process, ADP helps maintain equilibrium, and the type of nucleotide dictates structural transitions. Different species exhibit heterogeneity: Bacillus depends on high divalent ion concentrations and pH sensitivity, S. pneumoniae forms pH-Mg²⁺-dependent lateral interactions via its positively charged C-terminal domain, and T. maritima relies on nucleotide cycling for low critical concentration adaptation across temperatures. These findings highlight the evolutionary plasticity and environmentally adaptive molecular design in prokaryotic morphogenesis networksCC BY · PubMed Central
Fig. 7 Pharmacological Targeting of MreB and Resulting Cellular Morphological Changes. A22 and Mp265 competitively inhibit the binding of ATP to MreB, causing rapid depolymerization of MreB filaments in vivo and leading to a morphological shift of E. coli from rod-shaped to spherical. In contrast, CptA (YgfX) directly blocks the polymerization of MreB and FtsZ, resulting in cell swelling and a lemon-shaped appearance in E. coli
Fig. 7 Pharmacological Targeting of MreB and Resulting Cellular Morphological Changes. A22 and Mp265 competitively inhibit the binding of ATP to MreB, causing rapid depolymerization of MreB filaments in vivo and leading to a morphological shift of E. coli from rod-shaped to spherical. In contrast, CptA (YgfX) directly blocks the polymerization of MreB and FtsZ, resulting in cell swelling and a lemon-shaped appearance in E. coliCC BY · PubMed Central
Fig. 8 MreB interaction network and functional outcomes. MreB’s role in core network formation, antibacterial targeting, environmental responses, and function outputs, detailing specific interactions and outcomes
Fig. 8 MreB interaction network and functional outcomes. MreB’s role in core network formation, antibacterial targeting, environmental responses, and function outputs, detailing specific interactions and outcomesCC BY · PubMed Central

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Metadata

Authors
Wang, Y., jiang, Y., Song, Z., Zhu, C., Tang, Y., Peng, J., & Liu, P.
Affiliations
  • University of South China (CN)
  • Hengyang Normal University (CN)
Corresponding author
  • Peng, Jiaofeng
  • Liu, Peng
ORCID
Venue
Cell Communication and Signaling
Publisher
Springer Science and Business Media LLC
Published
2025-08-22
Volume
23
Issue
1
Pages
377-377
ISSN
1478-811X (ISSN-L)
DOI
10.1186/s12964-025-02373-y
PMC
PMC12372405
OpenAlex
W4413440625
Cited by
12
References
114
Citations by year
2026: 9 · 2025: 3
FWCI
1.84
Type
journal article
Language
en
Open access
Licence
Locations
  • Cell Communication and Signaling (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Guidance Plan Project of Hengyang City, China (2424017529)
  • National Natural Science Foundation of China (32370209)
  • Natural Science Foundation of Hunan Province, China (2023JJ30503)
  • The Scientific Research Foundation of Hunan Provincial Education Department, China (22A0297)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
MreB, bacterial cytoskeleton, actin-like protein, bacterial cell shape, cell division, peptidoglycan biosynthesis, chromosome segregation, RodZ, FtsZ, ion gradients, temperature sensitivity, environmental adaptation, antibiotic targets, bacterial self-organization
MeSH terms
Adaptation, Physiological, Bacteria, Bacterial Proteins, Cell Division, Cytoskeletal Proteins, Environment, Escherichia coli Proteins

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CoChat. (2026). Citation check: MreB: unraveling the molecular mechanisms of bacterial shape, division, and environmental adaptation. https://app.cochat.ai/papers/10.1186/s12964-025-02373-y
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Wang, Y., jiang, Y., Song, Z., Zhu, C., Tang, Y., Peng, J., & Liu, P. (2025). MreB: unraveling the molecular mechanisms of bacterial shape, division, and environmental adaptation. Cell Communication and Signaling. https://doi.org/10.1186/s12964-025-02373-y