Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation
The assembly and spatial organization of flagellar basal bodies in Escherichia coli are crucial for motility and chemotaxis. Using fluorescence and single-molecule microscopy, we demonstrate that key basal body proteins, FliF and FlhA, self-organize into clusters from low to high expression conditio...
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Elsevier
2025-06-01
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| Series: | Biochemistry and Biophysics Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580825001384 |
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| author | Yun-Sing Sung De-Fa Hong Yi-Ren Chang |
| author_facet | Yun-Sing Sung De-Fa Hong Yi-Ren Chang |
| author_sort | Yun-Sing Sung |
| collection | DOAJ |
| description | The assembly and spatial organization of flagellar basal bodies in Escherichia coli are crucial for motility and chemotaxis. Using fluorescence and single-molecule microscopy, we demonstrate that key basal body proteins, FliF and FlhA, self-organize into clusters from low to high expression conditions. Rather than forming new basal bodies, excess proteins accumulate around pre-existing structures, suggesting an autocatalytic mechanism. It is confirmed that clustering occurs even at low protein levels, indicating an intrinsic organizational principle rather than an artifact of overexpression. Fluorescence recovery after photobleaching (FRAP) revealed dynamic protein exchange within clusters, supporting a diffusion-capture model. Single-molecule analysis showed that FlhA actively remodels clusters, while FliF stabilizes them. 3D imaging suggested that basal body positioning optimizes flagellar distribution for efficient motility. These findings highlight a robust mechanism that regulates basal body positioning and flagellar assembly, ensuring adaptability to varying cellular conditions. |
| format | Article |
| id | doaj-art-e969be7225fc4f2a84f10669fd905817 |
| institution | OA Journals |
| issn | 2405-5808 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj-art-e969be7225fc4f2a84f10669fd9058172025-08-20T02:37:46ZengElsevierBiochemistry and Biophysics Reports2405-58082025-06-014210205110.1016/j.bbrep.2025.102051Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulationYun-Sing Sung0De-Fa Hong1Yi-Ren Chang2Department of Physics, National Taiwan Normal University, Taipei, 116, TaiwanDepartment of Physics, National Taiwan Normal University, Taipei, 116, TaiwanCorresponding author. 88, Sec.4, Ting-Chou Rd., Taipei, 116, Taiwan.; Department of Physics, National Taiwan Normal University, Taipei, 116, TaiwanThe assembly and spatial organization of flagellar basal bodies in Escherichia coli are crucial for motility and chemotaxis. Using fluorescence and single-molecule microscopy, we demonstrate that key basal body proteins, FliF and FlhA, self-organize into clusters from low to high expression conditions. Rather than forming new basal bodies, excess proteins accumulate around pre-existing structures, suggesting an autocatalytic mechanism. It is confirmed that clustering occurs even at low protein levels, indicating an intrinsic organizational principle rather than an artifact of overexpression. Fluorescence recovery after photobleaching (FRAP) revealed dynamic protein exchange within clusters, supporting a diffusion-capture model. Single-molecule analysis showed that FlhA actively remodels clusters, while FliF stabilizes them. 3D imaging suggested that basal body positioning optimizes flagellar distribution for efficient motility. These findings highlight a robust mechanism that regulates basal body positioning and flagellar assembly, ensuring adaptability to varying cellular conditions.http://www.sciencedirect.com/science/article/pii/S2405580825001384Flagellar assemblyProtein self-organizationSpatial regulationFluorescence super-resolution imagingSingle-molecule methods |
| spellingShingle | Yun-Sing Sung De-Fa Hong Yi-Ren Chang Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation Biochemistry and Biophysics Reports Flagellar assembly Protein self-organization Spatial regulation Fluorescence super-resolution imaging Single-molecule methods |
| title | Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation |
| title_full | Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation |
| title_fullStr | Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation |
| title_full_unstemmed | Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation |
| title_short | Intrinsic clustering of flagellar basal body proteins in E. coli: A self-organization mechanism for assembly and regulation |
| title_sort | intrinsic clustering of flagellar basal body proteins in e coli a self organization mechanism for assembly and regulation |
| topic | Flagellar assembly Protein self-organization Spatial regulation Fluorescence super-resolution imaging Single-molecule methods |
| url | http://www.sciencedirect.com/science/article/pii/S2405580825001384 |
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