Rice RuBisCO activase promotes the dark‐induced leaf senescence by enhancing the degradation of filamentation temperature‐sensitive H

Leaf senescence is a complex process that is triggered by many developmental and environmental factors. However, the mechanisms regulating leaf senescence remain unclear. Here, we revealed that rice ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) promotes the onset of basal dark-induced senescence. RCA was mainly expressed in the leaves, and its expression level quickly declined under dark conditions. Furthermore, rca mutant plants presented a prolonged leaf longevity phenotype in the dark, whereas overexpression of the large isoform of RCA (RCA<sub>L</sub>), not small isoform (RCA<sub>S</sub>), in rice and Arabidopsis accelerated leaf senescence. Filamentation temperature-sensitive H (OsFtsH1), a zinc metalloprotease, interacts with RCA<sub>L</sub> and RCA<sub>S</sub> and presents a higher binding efficiency to RCA<sub>L</sub> than RCA<sub>S</sub> in darkness. Furthermore, we found that RCA<sub>L</sub> promotes 26S proteasome-mediated degradation of OsFtsH1 protein, which can be inhibited by protease inhibitor MG132. Consequently, OsFtsH1 loss-of-function mutants exhibit accelerated leaf senescence, whereas OsFtsH1-overexpressing plants display delayed senescence. Collectively, our findings highlight the significant role of RCA<sub>L</sub> isoform in regulating leaf senescence under dark conditions, particularly through enhancing the degradation of OsFtsH1.

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Publication Details

Journal
The Plant Journal
Published
2025-02-01
DOI
https://doi.org/10.1111/tpj.17267
Citations
1
Primary Topic
Plant Stress Responses and Tolerance
Type
article
Field-Weighted Citation Impact
1.75

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article

Rice RuBisCO activase promotes the dark‐induced leaf senescence by enhancing the degradation of filamentation temperature‐sensitive H

Yaohuang Jiang, Yanli Zhang, Banpu Ruan, Xianrui Wu et al.
1 citations
The Plant Journal
Plant Stress Responses and Tolerance
1.75
article

Rice RuBisCO activase promotes the dark‐induced leaf senescence by enhancing the degradation of filamentation temperature‐sensitive H

Yaohuang Jiang, Yanli Zhang, Banpu Ruan, Xianrui Wu, Yanchun Yu, Yao‐Wu Yuan, Ying Zhang, Lu Liu, Fei Chen, Jian Wei, Limin Wu, Qian Qian, Guojun Dong
article en
1 citations

Abstract

Leaf senescence is a complex process that is triggered by many developmental and environmental factors. However, the mechanisms regulating leaf senescence remain unclear. Here, we revealed that rice ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) promotes the onset of basal dark-induced senescence. RCA was mainly expressed in the leaves, and its expression level quickly declined under dark conditions. Furthermore, rca mutant plants presented a prolonged leaf longevity phenotype in the dark, whereas overexpression of the large isoform of RCA (RCA<sub>L</sub>), not small isoform (RCA<sub>S</sub>), in rice and Arabidopsis accelerated leaf senescence. Filamentation temperature-sensitive H (OsFtsH1), a zinc metalloprotease, interacts with RCA<sub>L</sub> and RCA<sub>S</sub> and presents a higher binding efficiency to RCA<sub>L</sub> than RCA<sub>S</sub> in darkness. Furthermore, we found that RCA<sub>L</sub> promotes 26S proteasome-mediated degradation of OsFtsH1 protein, which can be inhibited by protease inhibitor MG132. Consequently, OsFtsH1 loss-of-function mutants exhibit accelerated leaf senescence, whereas OsFtsH1-overexpressing plants display delayed senescence. Collectively, our findings highlight the significant role of RCA<sub>L</sub> isoform in regulating leaf senescence under dark conditions, particularly through enhancing the degradation of OsFtsH1.

The Plant JournalVol. 121(4)
University of Connecticut (US), Hangzhou Normal University (CN), Jilin Agricultural University (CN), China National Rice Research Institute (CN)
National Natural Science Foundation of China, Natural Science Foundation of Zhejiang Province
Life in Land
Openalex Percentile: Top 17%
Plant Stress Responses and Tolerance
1.75
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