AtPRMT5 Regulates Shoot Regeneration through Mediating Histone H4R3 Dimethylation on KRPs and Pre-mRNA Splicing of RKP in Arabidopsis

• Published in: Molecular plant 2016-12, Vol.9 (12), p.1634-1646
• Main Authors: Liu, Hui, Ma, Xu, Han, Hua Nan, Hao, Yu Jin, Zhang, Xian Sheng
• Format: Article
• Language: English
• Subjects: Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Gene Expression Regulation, Plant - genetics; Gene Expression Regulation, Plant - physiology; histone modification; Histones - metabolism; Methylation; Plant Roots - genetics; Plant Roots - metabolism; Plant Shoots - genetics; Plant Shoots - metabolism; pre-mRNA splicing; protein arginine methylation; Protein-Arginine N-Methyltransferases - genetics; Protein-Arginine N-Methyltransferases - metabolism; RNA Splicing - genetics; RNA Splicing - physiology; RNA, Messenger - metabolism; RNA剪接; shoot regeneration; 介导; 愈伤组织; 拟南芥; 甲基转移酶; 组蛋白修饰; 细胞周期蛋白; 芽再生
• ISSN: 1674-2052; 1752-9867
• DOI: 10.1016/j.molp.2016.10.010

Protein arginine methylation plays important roles in diverse biological processes, but its role in regulating shoot regeneration remains elusive. In this study, we characterized the function of the protein arginine methyltransferase AtPRMT5 during de novo shoot regeneration in Arabidopsis. AtPRMT5 encodes a type II protein arginine methyltransferase that methylates proteins, including histories and RNA splicing factors. The frequency of shoot regeneration and the number of shoots per callus were decreased in the atprmt5 mutant compared with those in the wild type. Chromatin immunoprecipitation analysis revealed that AtPRMT5 targets KIP-RELATED PROTEINs （KRPs）, which encode the cyclin-dependent kinase inhibitors that repress the cell cycle. During shoot regeneration, the KRP transcript level increased in the atprmt5 mutant, which resulted from reduced histone H4R3 methylation in the KRP promoter. Overexpression of KRP significantly reduced the frequency of shoot regeneration and shoot number per callus. Furthermore, abnormal pre-mRNA splicing in the gene RELATED TO KPC1 （RKP）, which encodes an ubiquitin E3 ligase, was detected in the atprmt5 mutant. RKP functions in regulating KRP protein degradation, and mutation in RKP inhibited shoot regeneration. Thus, AtPRMT5 regulated shoot regeneration through histone modification-mediated KRP transcription and RKP pre-mRNA splicing. Our findings provide new insights into the function of protein arginine methylation in de novo shoot regeneration.