{"title":"肽激素RGF1通过活性氧依赖的半胱氨酸残基调节PLETHORA2的稳定性。","authors":"Yu-Chun Hsiao, Shiau-Yu Shiue, Ming-Ren Yen, Joon-Keat Lai, Masashi Yamada","doi":"10.1093/plphys/kiaf244","DOIUrl":null,"url":null,"abstract":"<p><p>The Root meristem growth factor 1 (RGF1) peptide extends the PLETHORA2 (PLT2) protein gradient by altering the distinct localization of superoxide (O2-) and hydrogen peroxide (H2O2) among the root developmental zones. However, the underlying mechanism through which reactive oxygen species (ROS) regulate PLT2 stability is unclear. Here, we demonstrate that the 212th cysteine of PLT2 is pivotal in modulating PLT2 stability through ROS. The PLT2 protein concentration gradient rapidly decreases in the elongation zone, where H2O2 accumulation initiates. However, substituting the 212th cysteine of PLT2 with serine (PLT2C212S) results in PLT2 being more stable in the elongation zone, more broadly localized by RGF1, and showing robust resistance to H2O2. The sulfenylation of PLT2 was detected following treatment with H2O2 at high concentrations, suggesting that S-sulfenylation of the 212th cysteine controls PLT2 protein stability through local ROS distributions. These findings show that the formation of the PLT2 concentration gradient through ROS depends on a PLT2 sulfenylation mechanism that involves the 212th cysteine.</p>","PeriodicalId":20101,"journal":{"name":"Plant Physiology","volume":"198 3","pages":""},"PeriodicalIF":6.5000,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The peptide hormone RGF1 modulates PLETHORA2 stability via reactive oxygen species-dependent regulation of a cysteine residue.\",\"authors\":\"Yu-Chun Hsiao, Shiau-Yu Shiue, Ming-Ren Yen, Joon-Keat Lai, Masashi Yamada\",\"doi\":\"10.1093/plphys/kiaf244\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The Root meristem growth factor 1 (RGF1) peptide extends the PLETHORA2 (PLT2) protein gradient by altering the distinct localization of superoxide (O2-) and hydrogen peroxide (H2O2) among the root developmental zones. However, the underlying mechanism through which reactive oxygen species (ROS) regulate PLT2 stability is unclear. Here, we demonstrate that the 212th cysteine of PLT2 is pivotal in modulating PLT2 stability through ROS. The PLT2 protein concentration gradient rapidly decreases in the elongation zone, where H2O2 accumulation initiates. However, substituting the 212th cysteine of PLT2 with serine (PLT2C212S) results in PLT2 being more stable in the elongation zone, more broadly localized by RGF1, and showing robust resistance to H2O2. The sulfenylation of PLT2 was detected following treatment with H2O2 at high concentrations, suggesting that S-sulfenylation of the 212th cysteine controls PLT2 protein stability through local ROS distributions. These findings show that the formation of the PLT2 concentration gradient through ROS depends on a PLT2 sulfenylation mechanism that involves the 212th cysteine.</p>\",\"PeriodicalId\":20101,\"journal\":{\"name\":\"Plant Physiology\",\"volume\":\"198 3\",\"pages\":\"\"},\"PeriodicalIF\":6.5000,\"publicationDate\":\"2025-07-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Physiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1093/plphys/kiaf244\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Physiology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/plphys/kiaf244","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
The peptide hormone RGF1 modulates PLETHORA2 stability via reactive oxygen species-dependent regulation of a cysteine residue.
The Root meristem growth factor 1 (RGF1) peptide extends the PLETHORA2 (PLT2) protein gradient by altering the distinct localization of superoxide (O2-) and hydrogen peroxide (H2O2) among the root developmental zones. However, the underlying mechanism through which reactive oxygen species (ROS) regulate PLT2 stability is unclear. Here, we demonstrate that the 212th cysteine of PLT2 is pivotal in modulating PLT2 stability through ROS. The PLT2 protein concentration gradient rapidly decreases in the elongation zone, where H2O2 accumulation initiates. However, substituting the 212th cysteine of PLT2 with serine (PLT2C212S) results in PLT2 being more stable in the elongation zone, more broadly localized by RGF1, and showing robust resistance to H2O2. The sulfenylation of PLT2 was detected following treatment with H2O2 at high concentrations, suggesting that S-sulfenylation of the 212th cysteine controls PLT2 protein stability through local ROS distributions. These findings show that the formation of the PLT2 concentration gradient through ROS depends on a PLT2 sulfenylation mechanism that involves the 212th cysteine.
期刊介绍:
Plant Physiology® is a distinguished and highly respected journal with a rich history dating back to its establishment in 1926. It stands as a leading international publication in the field of plant biology, covering a comprehensive range of topics from the molecular and structural aspects of plant life to systems biology and ecophysiology. Recognized as the most highly cited journal in plant sciences, Plant Physiology® is a testament to its commitment to excellence and the dissemination of groundbreaking research.
As the official publication of the American Society of Plant Biologists, Plant Physiology® upholds rigorous peer-review standards, ensuring that the scientific community receives the highest quality research. The journal releases 12 issues annually, providing a steady stream of new findings and insights to its readership.