{"title":"在拟南芥中,WRKY63的动态乙酰化受到HAG1和HDA6的拮抗调控","authors":"Yuan-Hsin Shih, Pei-Yu Lin, Fu-Yu Hung, Keqiang Wu","doi":"10.1111/tpj.70495","DOIUrl":null,"url":null,"abstract":"<div>\n \n <p>Lysine acetylation is a crucial post-translational modification that regulates protein function, stability, and subcellular localization. While extensively studied in mammalian systems, its role in plants remains largely unexplored. In this study, we identify the histone acetyltransferase HAG1 and the histone deacetylase HDA6 as key antagonistic regulators of the transcription factor WRKY63 acetylation. Using bimolecular fluorescence complementation assays, split-luciferase assays, and co-immunoprecipitation assays, we demonstrate that WRKY63 interacts with HAG1 and HDA6. Furthermore, the N-terminal region of WRKY63 is essential for these interactions. HAG1-mediated acetylation enhances WRKY63 nuclear localization, whereas HDA6-mediated deacetylation reduces its nuclear retention. Moreover, transient transcriptional assays indicate that HDA6 represses WRKY63-mediated transcriptional activation. Our findings highlight the broader significance of lysine acetylation beyond histone modification, uncovering an antagonistic regulatory network that fine-tunes transcription factor activity in plants.</p>\n </div>","PeriodicalId":233,"journal":{"name":"The Plant Journal","volume":"123 6","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2025-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Dynamic acetylation of WRKY63 is antagonistically regulated by HAG1 and HDA6 in Arabidopsis thaliana\",\"authors\":\"Yuan-Hsin Shih, Pei-Yu Lin, Fu-Yu Hung, Keqiang Wu\",\"doi\":\"10.1111/tpj.70495\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n <p>Lysine acetylation is a crucial post-translational modification that regulates protein function, stability, and subcellular localization. While extensively studied in mammalian systems, its role in plants remains largely unexplored. In this study, we identify the histone acetyltransferase HAG1 and the histone deacetylase HDA6 as key antagonistic regulators of the transcription factor WRKY63 acetylation. Using bimolecular fluorescence complementation assays, split-luciferase assays, and co-immunoprecipitation assays, we demonstrate that WRKY63 interacts with HAG1 and HDA6. Furthermore, the N-terminal region of WRKY63 is essential for these interactions. HAG1-mediated acetylation enhances WRKY63 nuclear localization, whereas HDA6-mediated deacetylation reduces its nuclear retention. Moreover, transient transcriptional assays indicate that HDA6 represses WRKY63-mediated transcriptional activation. Our findings highlight the broader significance of lysine acetylation beyond histone modification, uncovering an antagonistic regulatory network that fine-tunes transcription factor activity in plants.</p>\\n </div>\",\"PeriodicalId\":233,\"journal\":{\"name\":\"The Plant Journal\",\"volume\":\"123 6\",\"pages\":\"\"},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2025-09-26\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Plant Journal\",\"FirstCategoryId\":\"2\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/tpj.70495\",\"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":"The Plant Journal","FirstCategoryId":"2","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/tpj.70495","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
Dynamic acetylation of WRKY63 is antagonistically regulated by HAG1 and HDA6 in Arabidopsis thaliana
Lysine acetylation is a crucial post-translational modification that regulates protein function, stability, and subcellular localization. While extensively studied in mammalian systems, its role in plants remains largely unexplored. In this study, we identify the histone acetyltransferase HAG1 and the histone deacetylase HDA6 as key antagonistic regulators of the transcription factor WRKY63 acetylation. Using bimolecular fluorescence complementation assays, split-luciferase assays, and co-immunoprecipitation assays, we demonstrate that WRKY63 interacts with HAG1 and HDA6. Furthermore, the N-terminal region of WRKY63 is essential for these interactions. HAG1-mediated acetylation enhances WRKY63 nuclear localization, whereas HDA6-mediated deacetylation reduces its nuclear retention. Moreover, transient transcriptional assays indicate that HDA6 represses WRKY63-mediated transcriptional activation. Our findings highlight the broader significance of lysine acetylation beyond histone modification, uncovering an antagonistic regulatory network that fine-tunes transcription factor activity in plants.
期刊介绍:
Publishing the best original research papers in all key areas of modern plant biology from the world"s leading laboratories, The Plant Journal provides a dynamic forum for this ever growing international research community.
Plant science research is now at the forefront of research in the biological sciences, with breakthroughs in our understanding of fundamental processes in plants matching those in other organisms. The impact of molecular genetics and the availability of model and crop species can be seen in all aspects of plant biology. For publication in The Plant Journal the research must provide a highly significant new contribution to our understanding of plants and be of general interest to the plant science community.