bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Апрель 7, 2024

Abstract Our understanding of the functional requirements underpinning biomolecular condensation in vivo is still relatively poor. The Arabidopsis RNA binding protein FCA found liquid-like nuclear condensates that function transcription termination, promoting proximal polyadenylation at many targets genome. To further understand properties these we used single particle tracking experiments on reporters stably expressed endogenous levels plant nuclei. These revealed forms a core oligomer ∼4 molecules multimerizes into higher-order particles. This assembles macromolecular through coiled-coil FLL2, which genetically required for function. FLL2 predominately co-localizes with larger sized condensates. A missense mutation RRM domain, also function, reduced both average and condensate size but did not perturb oligomer. work points to modular structure involving multimerization oligomers assemble via associated interactions.

Язык: Английский