https://scholar.dgist.ac.kr/handle/20.500.11750/11725 Tue, 01 Sep 2026 19:46:02 GMT 2026-09-01T19:46:02Z https://scholar.dgist.ac.kr/handle/20.500.11750/60685 Title: Arabidopsis WSS1A, a DNA-protein crosslink repair protease, delays leaf senescence in cooperation with SUMO3 Author(s): Park, Sanghoon; Oh, Hyunwoo; Jeong, Ukcheol; Lee, Jae Ho; Choi, Hyeyoung; Park, Hyunsu; Kim, Jinkwang; Kim, Yongmin; Kwak, Junmin; Yoon, Yeong Seon; Li, Zhonghai; Lee, Jong-Chan; Woo, Hye Ryun Abstract: Leaf senescence, the final stage of leaf development, is regulated by complex interplays of intrinsic genetic programs and environmental cues. Throughout their lifetimes, all living organisms encounter various endogenous and environmental challenges, many of which can cause potentially fatal DNA damage. Among these, DNA-protein crosslinks (DPCs) are particularly deleterious, as they obstruct essential processes such as replication and transcription, thereby compromising genome integrity and ultimately leading to premature aging across species. However, the biological significance of DPCs and their repair mechanisms in leaf senescence remains unexplored. Here, we demonstrate that cis-platin (cis-Pt), a potent DPC inducer, accelerates leaf senescence in Arabidopsis. We reveal that Arabidopsis DPC repair factor WSS1A, a WLM/Spr-T metalloprotease, plays a negative role in leaf senescence induced by cis-Pt treatment, darkness, and leaf age. WSS1A forms nuclear condensates via liquid-liquid phase separation both in vitro and in vivo, which is cooperatively driven by its N-terminal segment and intrinsically disordered region. Mechanistically, WSS1A non-covalently interacts with SMALL UBIQUITIN MODIFIER 3 (SUMO3) through its SUMO-interacting motif and is also covalently SUMOylated by SUMO3. Genetic analysis further reveals that WSS1A and SUMO3 act in the same pathway to control cis-Pt-induced leaf senescence. Together, this study establishes a conceptual framework connecting DPC repair and SUMO3-dependent regulation of WSS1A in modulating leaf senescence in Arabidopsis. Fri, 31 Jul 2026 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/60685 2026-07-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/58316 Title: The kinase ATM delays Arabidopsis leaf senescence by stabilizing the phosphatase MKP2 in a phosphorylation-dependent manner Author(s): Zhang, Yi; Tan, Shuya; Kim, Jin Hee; Cao, Jie; Zhao, Yaning; Pang, Zhenpei; Liu, Junjie; Lv, Yonglun; Ding, Feng; Kim, Jeongsik; Woo, Hye Ryun; Xia, Xinli; Guo, Hongwei; Li, Zhonghai Abstract: Arabidopsis thaliana (Arabidopsis) Ataxia Telangiectasia Mutated (ATM) kinase plays a vital role in orchestrating leaf senescence; however, the precise mechanisms remain elusive. Here, our study demonstrates that ATM kinase activity is essential for mitigating age- and reactive oxygen species-induced senescence, as restoration of wild-type ATM reverses premature senescence in the atm mutant, while a kinase-dead ATM variant is ineffective. ATM physically interacts with and phosphorylates Mitogen-Activated Protein Kinase Phosphatase 2 (MKP2) to enhance stability under oxidative stress. Mutations in putative phosphorylation sites S15/154 on MKP2 disrupt its phosphorylation, stability, and senescence-delaying function. Moreover, mutation of mitogen-activated protein kinase 6, a downstream target of MKP2, alleviates the premature senescence phenotype of the atm mutant. Notably, the dual-specificity protein phosphatase 19 (HsDUSP19), a predicted human counter protein of MPK2, interacts with both ATM and HsATM and extends leaf longevity in Arabidopsis when overexpressed. These findings elucidate the molecular mechanisms underlying the role of ATM in leaf senescence and suggest that the ATM-MKP2 module is likely evolutionarily conserved in regulating the aging process across eukaryotes. © The Author(s) 2025. Mon, 31 Mar 2025 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/58316 2025-03-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/58242 Title: Emerging Regulatory Mechanisms of Leaf Senescence: Insights into Epigenetic Regulators, Non-Coding RNAs, and Peptide Hormones Author(s): Jeong, Ukcheol; Lim, Pyung Ok; Woo, Hye Ryun Abstract: Leaf senescence, the final phase of leaf development, plays a crucial role in plant fitness and crop improvement, as it enables nutrient remobilization from leaves to reproductive organs like developing seeds. This process involves extensive reprogramming of gene expression, governed by intricate regulatory networks operating across multiple layers of control. The employment of systems approaches using omics-based technologies and the characterization of key regulators has been instrumental in uncovering newly emerging regulatory mechanisms, providing valuable insights into how this orderly degeneration process is fine-tuned. In this review, we present a comprehensive overview of the current research on epigenetic mechanisms as a key layer within regulatory networks, influencing transcription factor activity and modulating the expression of senescence-associated genes. We also discuss recent advances in identifying the role of non-coding RNAs, RNA methylation, and peptide hormones during leaf senescence, which contributes to a deeper understanding of the complex regulatory pathways involved. Fri, 31 Jan 2025 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/58242 2025-01-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/56879 Title: Exploring the feasibility of a single-protoplast proteomic analysis Author(s): Vu, Minh Hung; Lee, Ju Yeon; Kim, Yongmin; Park, Sanghoon; Izaguirre, Fabiana; Lee, Juhyeon; Lee, Jung-Hyun; Jo, Minjoung; Woo, Hye Ryun; Kim, Jin Young; Lim, Pyung Ok; Kim, Min-Sik Abstract: Background: Recent advances in high-resolution mass spectrometry have now enabled the study of proteomes at the single-cell level, offering the potential to unveil novel aspects of cellular processes. Remarkably, there has been no prior attempt to investigate single-plant cell proteomes. In this study, we aimed to explore the feasibility of conducting a proteomic analysis on individual protoplasts. Findings: As a result, our analysis identified 978 proteins from the 180 protoplasts, aligning with well-known biological processes in plant leaves, such as photosynthetic electron transport in photosystem II. Employing the SCP package in the SCoPE2 workflow revealed a notable batch effect and extensive missing values in the data. Following correction, we observed the heterogeneity in single-protoplast proteome expression. Comparing the results of single-protoplast proteomics with those of bulk leaf proteomics, we noted that only a small fraction of bulk data was detected in the single-protoplast proteomics data, highlighting a technical limitation of the current single-cell proteomics method. Conclusions: In summary, we demonstrated the feasibility of conducting a single-protoplast proteomic experiment, revealing heterogeneity in plant cellular proteome expression. This underscores the importance of analyzing a substantial number of plant cells to discern statistically significant changes in plant cell proteomes upon perturbation such as abscisic acid treatment in future studies. We anticipate that our study will contribute to advancing single-protoplast proteomics in the near future. © The Author(s) 2024. Sun, 30 Jun 2024 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/56879 2024-06-30T15:00:00Z