Light-stabilized FHA2 suppresses miRNA biogenesis through interactions with DCL1 and HYL1
| Autor: | Seong Wook Yang, Sukwon Choi, Seung Jun Park, Hyun Sook Pai, Christian Møller, Gu Min Kim |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Ribonuclease III
0106 biological sciences 0301 basic medicine Light Cell Cycle Proteins Plant Science Biology 01 natural sciences Article law.invention 03 medical and health sciences Mirna expression law microRNA Molecular Biology miRNA biogenesis Arabidopsis Proteins Nuclear Proteins RNA-Binding Proteins MiRNA processing miRNA-biogenetic inconsistency Cell biology MicroRNAs Plant development 030104 developmental biology Mature mirnas Suppressor Suppressor of the microprocessor MiRNA biogenesis Biogenesis 010606 plant biology & botany |
| Zdroj: | Park, S J, Choi, S W, Kim, G M, Møller, C, Pai, H S & Yang, S W 2021, ' Light-stabilized FHA2 suppresses miRNA biogenesis through interactions with DCL1 and HYL1 ', Molecular Plant, vol. 14, no. 4, pp. 647-663 . https://doi.org/10.1016/j.molp.2021.01.020 Mol Plant |
| DOI: | 10.1016/j.molp.2021.01.020 |
| Popis: | The precise regulation of microRNA (miRNA) biogenesis is crucial for plant development, which requires core microprocessors and many fine tuners to coordinate their miRNA processing activity/specificity in fluctuating cellular environments. During de-etiolation, light triggers a dramatic accumulation of core microprocessors and primary miRNAs (pri-miRNAs) but decreases pri-miRNA processing activity, resulting in relatively constant miRNA levels. The mechanisms underlying these seemingly contradictory regulatory changes remain unclear. In this study, we identified forkhead-associated domain 2 (FHA2) as a light-stabilized suppressor of miRNA biogenesis. We found that FHA2 deficiency increased the level of mature miRNAs, accompanied by a reduction in pri-miRNAs and target mRNAs. Biochemical assays showed that FHA2 associates with the core microprocessors DCL1, HYL1, and SE, forming a complex to suppress their pri-miRNA processing activity. Further analyses revealed that FHA2 promotes HYL1 binding but inhibits the binding of DCL1-PAZ-RNase-RNA-binding domains (DCL1-PRR) to miRNAs, whereas FHA2 does not directly bind to these RNAs. Interestingly, we found that FHA2 protein is unstable in the dark but stabilized by light during de-etiolation. Consistently, disruption of FHA led to defects in light-triggered changes in miRNA expression and reduced the survival rate of de-etiolated seedlings after prolonged light deprivation. Collectively, these data suggest that FHA2 is a novel light-stabilized suppressor of miRNA biogenesis and plays a role in fine-tuning miRNA processing during de-etiolation. |
| Databáze: | OpenAIRE |
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