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Faturova, J.

Publications and source records attributed to Faturova, J..

3 recordsLinked to original sources

A Cajal body assembly factor regulates cell fate transitions in Arabidopsis

Ribonucleoprotein (RNP) condensates are emerging as key regulators of cell fate transitions, yet their functions have been largely linked to mRNA storage and translational control. Here, we uncover a role for Cajal body (CB)-mediated pre-mRNA splicing in coordinating the transition from stem cell divisions to differentiation in plants. We identify THREE-DIVISION MUTANT 3 (TDM3) as a cell cycle-regulated factor required for post-mitotic CB assembly. Loss of TDM3 or the CB scaffold protein COILIN delays differentiation and prolongs formative cell divisions. Transcriptome analysis revealed that TDM3 and COILIN jointly regulate pre-mRNA splicing, including transcripts controlling cell cycle and fate transitions. These findings establish CB-mediated splicing as a mechanism linking cell cycle progression to cellular differentiation.

cell biology↗

MO25 binds CBL-interacting protein kinases associated with ribonucleoprotein condensates and regulates meiotic exit

Meiotic (M)-bodies are multiphasic ribonucleoprotein (RNP) condensates composed of a P-body core surrounded by a stress granule-like shell that promote meiotic exit through transient translational repression. This process depends on the phosphoserine-binding protein SMG7, which recruits the meiotic regulator TDM1 to M-bodies during meiosis II. Here, we identify the evolutionarily conserved scaffold protein MO25 as a regulator of SMG7 and TDM1 partitioning into M-bodies in Arabidopsis thaliana. Disruption of MO25A1 enhances the accumulation of SMG7 and TDM1 in M-bodies and increases the reduced fertility in the hypomorphic smg7-6 mutant, which exhibits impaired M-body association. In fungi and animals, MO25 proteins act as allosteric activators of STE20-family kinases. Interaction screening revealed that, whereas Arabidopsis MO25B proteins interact with STE20-family MAP4K kinases, MO25A paralogues have evolved specificity toward a subset of CBL-interacting protein kinases (CIPKs). Notably, the MO25A-interacting CIPKs localize to diverse nuclear and cytoplasmic RNP condensates. Among them, CIPK6 is required for fertility and pollen development, and disruption of its MO25-binding domain enhances SMG7 condensation. Together, our findings identify a previously unrecognized MO25A-CIPK interaction module that regulates M-body organization and may more broadly contribute to the regulation of RNP condensates.

plant biology↗

Identification and characterization of a TRF2-like telomere-binding protein in Arabidopsis

Telomere protection and maintenance are mediated by proteins that bind telomeric DNA and recruit additional components of telomeric chromatin. While these factors are well characterized in yeast and mammals, their counterparts in plants remain poorly defined. Here, we used a proteomic approach in Arabidopsis thaliana to identify nuclear proteins that preferentially associate with telomeric DNA. We identified TRFL7, a previously uncharacterized member of the TRF-like (TRFL) protein family, as a prominent candidate. We show that TRFL7, together with its close homologues TRFL5 and TRFL11, associates with telomeric chromatin and forms distinct nuclear foci that preferentially localize near the nucleolus, resembling the nucleolus-associated telomere clustering characteristic of Arabidopsis. Genetic inactivation of TRFL7 in combination with either TRFL5 or TRFL11 results in telomere elongation, indicating a role for these proteins in telomere length homeostasis. Notably, TRFL7 contains an iDDR sequence motif that is also present in human TRF2, where it limits the activity of the Mre11-Rad50-Nbs1 complex. Together, our findings identify TRFL7 as a functional component of plant telomeric chromatin and suggest that it represents a plant orthologue of human TRF2.

molecular biology↗