APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in Arabidopsis thaliana

International Journal of Molecular Sciences, Год журнала: 2024, Номер 25(2), С. 1313 - 1313

Опубликована: Янв. 21, 2024

WD40 repeat proteins (WDRs) are present in all eukaryotes and include members that implicated numerous cellular activities. They act as scaffold thus molecular "hubs" for protein-protein interactions, which mediate the assembly of multifunctional complexes regulate key developmental processes Arabidopsis thaliana, such flowering time, hormonal signaling, stress responses. Despite their importance, many aspects putative functions have not been elucidated yet. Here, we show late-flowering phenotype anthesis promoting factor 1 (aprf1) mutants is temperature-dependent can be suppressed when plants grown under mild heat conditions. To gain further insight into mechanism APRF1 function, employed a co-immunoprecipitation (Co-IP) approach to identify its interaction partners. We provide first interactome APRF1, includes localized several subcellular compartments diverse functions. The dual nucleocytoplasmic localization ARRF1, was validated through with HEAT SHOCK PROTEIN (HSP90.1) nucleus HSP90.2 cytoplasm, indicates dynamic versatile involvement multiple biological processes. specific chaperon HSP90.1 expands our knowledge regarding epigenetic regulation time A. thaliana suggests existence delicate thermoregulated during anthesis.

Язык: Английский

In vivoproperties of Arabidopsis FCA condensates involved in RNA 3’ processing

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