| Bimetallic gold-silver nanoparticles mediate bacterial killing by disrupting the actin cytoskeleton MreB. | Bimetallic gold-silver nanoparticles mediate bacterial killing by disrupting the actin cytoskeleton MreB.
Jena P, Bhattacharya M, Bhattacharjee G, Satpati B, Mukherjee P, Senapati D, Srinivasan R. | 10/31/2020 |
| MreBA125V and MreBA174T mutant cells were thinner and thicker than WT cells, and MreBA125V and MreBA174T rotated faster and slower than WT, respectively. | Relation between rotation of MreB actin and cell width of Escherichia coli.
Kurita K, Shin R, Tabei T, Shiomi D. | 04/20/2019 |
| Studies indicate the function of dynamic cytoskeletal protein MreB to generate an integrated model of rod-shaped wall construction [Review]. | How to Build a Bacterial Cell: MreB as the Foreman of E. coli Construction.
Shi H, Bratton BP, Gitai Z, Huang KC., Free PMC Article | 01/26/2019 |
| MreB mutants alter the bending properties of MreB filaments in molecular dynamics simulations similar to RodZ binding, and these mutants rescue rod-like shape in the absence of RodZ alone or in combination with wild-type MreB. | RodZ modulates geometric localization of the bacterial actin MreB to regulate cell shape.
Colavin A, Shi H, Huang KC., Free PMC Article | 12/22/2018 |
| The data suggest that RodZ promotes the assembly of geometrically-localized MreB polymers that lead to the growth of uniform E. coli cylinders. | MreB polymers and curvature localization are enhanced by RodZ and predict E. coli's cylindrical uniformity.
Bratton BP, Shaevitz JW, Gitai Z, Morgenstein RM., Free PMC Article | 12/22/2018 |
| MreB is not recruited to the FtsZ ring in secA mutant cells, contributing to division arrest and cell filamentation.. Thus, when we reroute RodZ, MreB membrane-anchor, by fusing it to a SecA-independent integral membrane protein and overproducing it, MreB localization is restored and the defect in cell division is corrected. | The bacterial Sec system is required for the organization and function of the MreB cytoskeleton.
Govindarajan S, Amster-Choder O., Free PMC Article | 10/14/2017 |
| Although several other protein modulators are known to target FtsZ, the CbtA-interacting surface we identify represents a novel inhibitory target. Our findings establish CbtA as a dual function toxin that inhibits both cell division and cell elongation via direct and independent interactions with FtsZ and MreB. | CbtA toxin of Escherichia coli inhibits cell division and cell elongation via direct and independent interactions with FtsZ and MreB.
Heller DM, Tavag M, Hochschild A., Free PMC Article | 10/14/2017 |
| Results demonstrate that the physical properties of MreB filaments are important for shape control and support a model in which MreB organizes the cell wall growth machinery to produce a chiral cell wall structure and dictate cell diameter | MreB Orientation Correlates with Cell Diameter in Escherichia coli.
Ouzounov N, Nguyen JP, Bratton BP, Jacobowitz D, Gitai Z, Shaevitz JW., Free PMC Article | 07/8/2017 |
| E75, R78 and D82 of FtsZ are key residues for FtsZ self-assembly and FtsZ-MreB interaction. | [E75, R78 and D82 of Escherichia coli FtsZ are key residues for FtsZ cellular self-assembly and FtsZ-MreB interaction].
Huo Y, Lu Q, Zheng X, Ma Y, Lu F. | 07/30/2016 |
| Data show that actin homolog MreB rotates because cytoplasmic MreB filaments are coupled to periplasmic cell wall synthesis through the transmembrane protein RodZ, which acts as a transmembrane linker. | RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis.
Morgenstein RM, Bratton BP, Nguyen JP, Ouzounov N, Shaevitz JW, Gitai Z., Free PMC Article | 03/19/2016 |
| The tight regulation and fine-tuning of mreB gene expression in response to cellular stresses is discussed in regard to the effect of the MreB protein on cell elongation. | Riboregulation of the bacterial actin-homolog MreB by DsrA small noncoding RNA.
Cayrol B, Fortas E, Martret C, Cech G, Kloska A, Caulet S, Barbet M, Trépout S, Marco S, Taghbalout A, Busi F, Wegrzyn G, Arluison V. | 09/26/2015 |
| The discrete spatial distribution and dynamics of PspA effector in lateral membrane regions depend on MreB and RodZ. | Anionic lipids and the cytoskeletal proteins MreB and RodZ define the spatio-temporal distribution and function of membrane stress controller PspA in Escherichia coli.
Jovanovic G, Mehta P, Ying L, Buck M. | 06/27/2015 |
| Bacterial two-hybrid assay and accumulation of Gp0.6 only in MreB-expressing bacteria confirmed interaction of MreB and Gp0.6. Expression of Gp0.6 resulted in lemon-shaped bacteria followed by cell lysis | Revealing bacterial targets of growth inhibitors encoded by bacteriophage T7.
Molshanski-Mor S, Yosef I, Kiro R, Edgar R, Manor M, Gershovits M, Laserson M, Pupko T, Qimron U., Free PMC Article | 04/25/2015 |
| Defective N-acetylglucosamine catabolism and point mutations in MreB are associated with osmotolerant. | Evolved osmotolerant Escherichia coli mutants frequently exhibit defective N-acetylglucosamine catabolism and point mutations in cell shape-regulating protein MreB.
Winkler JD, Garcia C, Olson M, Callaway E, Kao KC., Free PMC Article | 01/31/2015 |
| MreB remains functional irrespective of its distribution being misguided by the aberrant shapes of PBP mutants. | PBP deletion mutants of Escherichia coli exhibit irregular distribution of MreB at the deformed zones.
Vijayan S, Mallick S, Dutta M, Narayani M, Ghosh AS. | 09/13/2014 |
| MreB orchestrates persistent, heterogeneous growth at the subcellular scale, enabling robust, uniform growth at the cellular scale without requiring global organization. | Rod-like bacterial shape is maintained by feedback between cell curvature and cytoskeletal localization.
Ursell TS, Nguyen J, Monds RD, Colavin A, Billings G, Ouzounov N, Gitai Z, Shaevitz JW, Huang KC., Free PMC Article | 05/31/2014 |
| MreB exhibits actin-like polymerization-dependent structural changes, wherein polymerization induces flattening of MreB subunits, which restructures the nucleotide-binding pocket to favor hydrolysis. | Effects of polymerization and nucleotide identity on the conformational dynamics of the bacterial actin homolog MreB.
Colavin A, Hsin J, Huang KC., Free PMC Article | 05/10/2014 |
| the fibrillation of MreB filaments can take place either in close proximity of deformable lipid membrane or in the presence of associated protein | Assembly of MreB filaments on liposome membranes: a synthetic biology approach.
Maeda YT, Nakadai T, Shin J, Uryu K, Noireaux V, Libchaber A. | 04/26/2014 |
| Mutations in mreB, mrdA and mrdB suppress the shape defect of RodZ-deficient cells. | Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ-deficient cells.
Shiomi D, Toyoda A, Aizu T, Ejima F, Fujiyama A, Shini T, Kohara Y, Niki H., Free PMC Article | 08/31/2013 |
| YeeU was found to directly interact with MreB and FtsZ, and enhance the bundling of their filamentous polymers in vitro and proposed to rename as CbeA for cytoskeleton bundling-enhancing factor A. | YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli.
Masuda H, Tan Q, Awano N, Wu KP, Inouye M. | 09/22/2012 |
| Data suggest that one function of MreB rotation is to ensure a uniform distribution of new peptidoglycan insertion sites, a necessary condition to maintain rod shape during growth. | The bacterial actin MreB rotates, and rotation depends on cell-wall assembly.
van Teeffelen S, Wang S, Furchtgott L, Huang KC, Wingreen NS, Shaevitz JW, Gitai Z., Free PMC Article | 12/17/2011 |
| The authors show that YeeV toxin inhibits cell division, leads to a change in morphology and lysis of Escherichia coli cells via interaction with two essential cytoskeleton proteins, FtsZ and MreB. | YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB.
Tan Q, Awano N, Inouye M., Free PMC Article | 04/9/2011 |
| MreB is rigidly linked to the cell wall, increasing its mechanical stiffness. | Actin-like cytoskeleton filaments contribute to cell mechanics in bacteria.
Wang S, Arellano-Santoyo H, Combs PA, Shaevitz JW., Free PMC Article | 07/26/2010 |
| Data show that MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. | In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2.
Varma A, Young KD., Free PMC Article | 01/21/2010 |
| alterations in cell morphology induced by bolA seem to be mediated by a complex pathway that integrates PBP5, PBP6, MreB, and probably other regulators of cell morphology/elongation. | BolA inhibits cell elongation and regulates MreB expression levels.
Freire P, Moreira RN, Arraiano CM. | 01/21/2010 |