StSIRT1 regulates potato dormancy through deacetylation of peroxidase-like 3 at K37
5 affiliations
- 1College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China.
- 2Key Laboratory of Agro-Products Postharvest Handling, Ministry of Agriculture and Rural Affairs, Zhejiang Key Laboratory of Agri-food Resources and High-value Utilization, Innovation Centre for Postharvest Agro-Products Technology, Zhejiang University, Hangzhou 310058, China.
- 3State Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Agronomy, Northwest A&F University, Yangling 712100, China.
- 4Sustainable and Smart Materials Laboratory, Department of Biomedical Engineering and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru 81310, Malaysia.
- 5Key Laboratory of Chemical and Biological Processing Technology for Farm Products of Zhejiang Province, Zhejiang Provincial Collaborative Innovation Centre of Agricultural Biological Resources Biochemical Manufacturing, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China.
Abstract
Plants have evolved sophisticated defense systems to synchronize growth with environmental fluctuations, including the adaptive strategy of dormancy, an important agronomic trait. Nevertheless, the role of posttranslational modification of nonhistone proteins in dormancy regulation remains elusive. Here, we report that sirtuin (StSIRT1)-mediated deacetylation of peroxidase (StPRX3) suppresses peroxidase activity, culminating in potato (Solanum tuberosum L.) dormancy release. The lysine deacetylase StSIRT1-suppressed by the dormancy regulator nicotinamide (NAM)-accumulates during dormancy release and negatively modulates StPRX3. Furthermore, lysine-37 (K37; K denotes lysine) in StPRX3 is essential for its direct interaction with StSIRT1. StSIRT1 interacts with StPRX3 to regulate the hydrogen peroxide (H₂O₂)-scavenging capacity of peroxidase by decreasing K37 acetylation levels. Notably, the StPRX3K37R (K37→arginine, K37R; R denotes arginine) mutant suppresses peroxidase activity, leading to accelerated potato dormancy release. Our findings uncover an StSIRT1-StPRX3 cascade in dormancy regulation that activates peroxidase and reduces H₂O₂ levels in potato, providing insights into the complex regulatory networks involved in dormancy.
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BibTeX
@article{hu2026stsirt1,
title = {{StSIRT1 regulates potato dormancy through deacetylation of peroxidase-like 3 at K37}},
author = {Qiannan Hu and Yingying Dong and Hongxia Hu and Yizhou Xiang and Bailin Liu and Tuck-Whye Wong and Zhaojun Ban and Zisheng Luo and Li Li},
journal = {Science Advances},
year = {2026},
month = oct,
doi = {10.1126/sciadv.aef7735},
url = {https://www.science.org/doi/abs/10.1126/sciadv.aef7735},
note = {CC BY},
}
RIS
TY - JOUR
TI - StSIRT1 regulates potato dormancy through deacetylation of peroxidase-like 3 at K37
AU - Qiannan Hu
AU - Yingying Dong
AU - Hongxia Hu
AU - Yizhou Xiang
AU - Bailin Liu
AU - Tuck-Whye Wong
AU - Zhaojun Ban
AU - Zisheng Luo
AU - Li Li
PY - 2026
DA - 2026/10/28
JO - Science Advances
DO - 10.1126/sciadv.aef7735
UR - https://www.science.org/doi/abs/10.1126/sciadv.aef7735
AB - Plants have evolved sophisticated defense systems to synchronize growth with environmental fluctuations, including the adaptive strategy of dormancy, an important agronomic trait. Nevertheless, the role of posttranslational modification of nonhistone proteins in dormancy regulation remains elusive. Here, we report that sirtuin (StSIRT1)-mediated deacetylation of peroxidase (StPRX3) suppresses peroxidase activity, culminating in potato (Solanum tuberosum L.) dormancy release. The lysine deacetylase StSIRT1-suppressed by the dormancy regulator nicotinamide (NAM)-accumulates during dormancy release and negatively modulates StPRX3. Furthermore, lysine-37 (K37; K denotes lysine) in StPRX3 is essential for its direct interaction with StSIRT1. StSIRT1 interacts with StPRX3 to regulate the hydrogen peroxide (H₂O₂)-scavenging capacity of peroxidase by decreasing K37 acetylation levels. Notably, the StPRX3K37R (K37→arginine, K37R; R denotes arginine) mutant suppresses peroxidase activity, leading to accelerated potato dormancy release. Our findings uncover an StSIRT1-StPRX3 cascade in dormancy regulation that activates peroxidase and reduces H₂O₂ levels in potato, providing insights into the complex regulatory networks involved in dormancy.
SN - 2375-2548
ER -