F-box protein CFK1 interacts with and degrades de novo DNA methyltransferase in Arabidopsis
文献类型： 外文期刊
作者： Chen, Jiani 1 ; Liu, Jie 1 ; Jiang, Jianjun 2 ; Qian, Shuiming 1 ; Song, Jingwen 4 ; Kabara, Rachel 2 ; Delo, Isabel 2 ;
作者机构： 1.Univ Wisconsin, Wisconsin Inst Discovery, Madison, WI 53715 USA
2.Univ Wisconsin, Lab Genet, Madison, WI 53706 USA
3.Jiangsu Acad Agr Sci, Jiangsu Key Lab Food Qual & Safety, State Key Lab Cultivat Base, Inst Plant Protect,Minist Sci & Technol, Nanjing 210014, Jiangsu, Peoples R China
4.Ohio Univ, Dept Environm & Plant Biol, Athens, OH 45701 USA
5.Ohio Univ, Interdisciplinary Program Mol & Cellular Biol, Athens, OH 45701 USA
6.Sapienza Univ Roma, Dept Biol & Biotechnol, I-00185 Rome, Italy
关键词： Arabidopsis thaliana; DNA methylation; epigenetics; F‐ box protein; post‐ translational modification; ubiquitin proteasome pathway
期刊名称：NEW PHYTOLOGIST （ 影响因子：10.151； 五年影响因子：10.475 ）
ISSN： 0028-646X
年卷期： 2021 年 229 卷 6 期
页码：
收录情况： SCI
摘要： DNA methylation plays crucial roles in cellular development and stress responses through gene regulation and genome stability control. Precise regulation of DOMAINS REARRANGED METHYLTRANSFERASE 2 (DRM2), the de novo Arabidopsis DNA methyltransferase, is crucial to maintain DNA methylation homeostasis to ensure genome integrity. Compared with the extensive studies on DRM2 targeting mechanisms, little information is known regarding the quality control of DRM2 itself. Here, we conducted yeast two-hybrid screen assay and identified an E3 ligase, COP9 INTERACTING F-BOX KELCH 1 (CFK1), as a novel DRM2-interacting partner and targets DRM2 for degradation via the ubiquitin-26S proteasome pathway in Arabidopsis thaliana. We also performed whole genome bisulfite sequencing (BS-seq) to determine the biological significance of CFK1-mediated DRM2 degradation. Loss-of-function CFK1 leads to increased DRM2 protein abundance and overexpression of CFK1 showed reduced DRM2 protein levels. Consistently, CFK1 overexpression induces genome-wide CHH hypomethylation and transcriptional de-repression at specific DRM2 target loci. This study uncovered a distinct mechanism regulating de novo DNA methyltransferase by CFK1 to control DNA methylation level.
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