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TitleThe filamentous ultrastructure of the PopZ condensate is required for its cellular function.
Journal, issue, pagesNat Struct Mol Biol, Vol. 33, Issue 3, Page 420-432, Year 2026
Publish dateFeb 2, 2026
AuthorsDaniel Scholl / Tumara Boyd / Andrew P Latham / Alexandra Salazar / Asma M A M Khan / Steven Boeynaems / Alex S Holehouse / Gabriel C Lander / Andrej Sali / Donghyun Park / Ashok A Deniz / Keren Lasker /
PubMed AbstractBiomolecular condensates have key roles in regulating cellular processes. Yet, the relationship between atomic features and condensate function remains poorly understood. We studied this relationship ...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.
External linksNat Struct Mol Biol / PubMed:41629604 / PubMed Central
MethodsEM (tomography)
Structure data

EMDB-47539: Representative tomogram of WT-PopZ condensate
Method: EM (tomography)

EMDB-47540: Representative tomogram of OD-PopZ condensate
Method: EM (tomography)

EMDB-47542: Representative tomogram of DL6-PopZ condensate
Method: EM (tomography)

Source
  • Caulobacter vibrioides (bacteria)

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