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Mol. Plant., Available online 29 January 2021 | https://doi.org/10.1016/j.molp.2021.01.020 Light-Stabilized FHA2 Suppresses miRNA Biogenesis through Interactions with DCL1 and HYL1

Seung Jun Park^1,†, Suk Won Choi^2,†, Gu Min Kim², Christian Møller², Hyun-Sook Pai^1,*, Seong Wook Yang^2,3,4,*

¹Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea
²Department of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea
³Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg, Copenhagen, Denmark
⁴Pohang University of Science and Technology (POSTECH), 77 Cheongam-Ro, Nam-Gu, Pohang, Gyeongbuk, 37673, Korea

^†These authors contributed equally to this article.

^*Corresponding author

Abstract

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 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 the 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.

논문정보

형식Research article
게재일2021년 01월 (BRIC 등록일 2021-02-03)
연구진국내(교신)+국외 연구진
분야 생명과학 > 분자생물학

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