Duncan NRI Faculty and Staff Publications
Language
English
Publication Date
3-1-2026
Journal
Nature Structural & Molecular Biology
DOI
10.1038/s41594-025-01742-y
PMID
41629604
PMCID
PMC12999525
PubMedCentral® Posted Date
2-2-2026
PubMedCentral® Full Text Version
Post-print
Abstract
Biomolecular condensates have key roles in regulating cellular processes. Yet, the relationship between atomic features and condensate function remains poorly understood. We studied this relationship using the polar organizing protein Z (PopZ). Here, we revealed hierarchical assembly of PopZ into a filamentous condensate by integrating cryo-electron tomography, biochemistry, single-molecule techniques and molecular dynamics simulations. The PopZ helical domain drives filamentation and condensation, while the disordered region inhibits them. Phase-dependent conformational changes prevent interfilament contacts in the dilute phase and expose client-binding sites in the dense phase. Perturbing filament formation in vitro alters the dynamics of scaffold and client proteins and the condensate's wetting behavior. In cells, perturbing either filament formation or the ability of filaments to condense impairs PopZ function and leads to growth phenotypes. These findings establish a multiscale framework linking molecular interactions and condensate ultrastructure to cellular function.
Keywords
Cryoelectron Microscopy, Molecular Dynamics Simulation, Electron Microscope Tomography, Biomolecular Condensates, Escherichia coli Proteins, Escherichia coli, Cellular microbiology, Molecular biophysics, Cell division, Cryoelectron tomography
Published Open-Access
yes
Recommended Citation
Scholl, Daniel; Boyd, Tumara; Latham, Andrew P; et al., "The Filamentous Ultrastructure of the PopZ Condensate Is Required for Its Cellular Function" (2026). Duncan NRI Faculty and Staff Publications. 205.
https://digitalcommons.library.tmc.edu/duncar_nri_pub/205
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