The RNA binding protein EHD6 recruits the m 6 A reader YTH07 and sequesters OsCOL4 mRNA into phase-separated ribonucleoprotein condensates to promote rice flowering

文献类型： 外文期刊

第一作者： Cui, Song

作者： Cui, Song;Wang, Chaolong;Chen, Saihua;Hao, Benyuan;Xu, Zhuang;Cai, Liang;Gan, Xiangchao;Dong, Hui;Hu, Yuan;Zhou, Liang;Hou, Haigang;Tian, Yunlu;Liu, Xi;Chen, Liangming;Liu, Shijia;Jiang, Ling;Zhou, Shirong;Wan, Jianmin;Cui, Song;Zhu, Shanshan;Wang, Haiyang;Wan, Jianmin;Song, Peizhe;Chen, Xu;Jia, Guifang;Chen, Saihua;Gan, Xiangchao

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关键词： N 6-methyladenosine; m 6 A; EHD6; YTH domain-containing protein; phase separation; heading date

期刊名称：MOLECULAR PLANT （ 影响因子：17.1； 五年影响因子：21.4 ）

ISSN： 1674-2052

年卷期： 2024 年 17 卷 6 期

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收录情况： SCI

摘要： N 6 -Methyladenosine (m 6 A) is one of the most abundant modifications of eukaryotic mRNA, but its comprehensive biological functionality remains further exploration. In this study, we identified and characterized a new flowering -promoting gene, EARLY HEADING DATE6 ( EHD6 ), in rice. EHD6 encodes an RNA recognition motif (RRM)-containing RNA binding protein that is localized in the non -membranous cytoplasm ribonucleoprotein (RNP) granules and can bind both m 6 A-modified RNA and unmodified RNA indiscriminately. We found that EHD6 can physically interact with YTH07, a YTH (YT521-B homology) domain -containing m 6 A reader. We showed that their interaction enhances the binding of an m 6 A-modified RNA and triggers relocation of a portion of YTH07 from the cytoplasm into RNP granules through phase -separated condensation. Within these condensates, the mRNA of a rice flowering repressor, CONSTANS-like 4 ( OsCOL4 ), becomes sequestered, leading to a reduction in its protein abundance and thus accelerated flowering through the Early heading date 1 pathway. Taken together, these results not only shed new light on the molecular mechanism of efficient m 6 A recognition by the collaboration between an RNA binding protein and YTH family m 6 A reader, but also uncover the potential for m 6 A-mediated translation regulation through phaseseparated ribonucleoprotein condensation in rice.

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