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Updated: May 31, 2026

mirMachine: A One-Stop Shop for Plant miRNA Annotation
Published on: May 1, 2021
Dehydration-induced condensation of AGO1 modulates miRNA functionality
Hyun Ju Jung1, Tae Rin Oh2, Woorim Yang1
1Department of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea.
Abstract:
Recent studies have shown that microRNA (miRNA) functions are associated with plant responses to water deficiency. Mature miRNAs are loaded onto a complex that includes the ARGONAUTE 1 (AGO1) protein; this complex then cleaves mRNAs or inhibits their translation. Here, we demonstrate that the prion-like domain of AGO1 is responsible for topological changes in AGO1 under dehydration in Arabidopsis thaliana. AGO1 undergoes liquid-liquid phase separation (LLPS), which is driven by intrinsically disordered protein domains and plays diverse roles in cellular processes. LLPS of AGO in the cytoplasm influences miRNA regulatory activity, a process related to cytoplasmic calcium levels. We found that dehydration-induced AGO1 condensation influences AGO1 activity, while contributing to dehydration tolerance in plants. Upon rehydration, the condensation-driven accumulation of AGO1 is resolved, restoring its protein levels to normal. Overall, we propose that AGO1 phase separation acts as an emergent property in response to dehydration, attenuating the energy-consuming miRNA regulatory pathway in young seedlings.
Insights
Plant dehydration tolerance is enhanced by ARGENTAUTE 1 (AGO1) protein phase separation, which temporarily reduces energy-intensive microRNA (miRNA) regulation during drought stress.
Area of Science:
- Plant Biology
- Molecular Biology
- Biochemistry
Background:
- MicroRNAs (miRNAs) regulate gene expression and are crucial for plant responses to environmental stresses like water deficiency.
- The ARGENTAUTE 1 (AGO1) protein is a key component of the miRNA-induced silencing complex, mediating mRNA cleavage or translational repression.
Purpose of the Study:
- To investigate the role of the ARGENTAUTE 1 (AGO1) protein's prion-like domain in plant responses to dehydration.
- To elucidate the mechanism by which AGO1 functions under water-deficient conditions in Arabidopsis thaliana.
Main Methods:
- Analysis of AGO1 protein behavior under dehydration stress in Arabidopsis thaliana.
- Investigating the phenomenon of liquid-liquid phase separation (LLPS) in AGO1.
- Assessing the impact of AGO1 condensation on miRNA regulatory activity and plant dehydration tolerance.
Main Results:
- The prion-like domain of AGO1 facilitates topological changes and liquid-liquid phase separation (LLPS) under dehydration.
- Dehydration-induced AGO1 condensation modulates its activity and enhances plant dehydration tolerance.
- AGO1 condensation is reversible upon rehydration, restoring normal protein levels and miRNA regulation.
Conclusions:
- AGO1 phase separation is an emergent property that helps plants cope with dehydration by attenuating energy-consuming miRNA pathways.
- This mechanism provides a novel insight into plant stress tolerance at the molecular level.
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