Selective recognition of PTRE1 transcripts mediated by protein-protein interaction between the m^(6)A reader ECT2 and PTRE1  

作　　者：Li Yang Bo Wang Duanmu Zhao Xuechun Li Yifei Qin Ning Ouyang Zhili Xiao Zhibing Zhang Gad Galili Jiayang Li Hadas Peled-Zehavi Jian Wu 

机构地区：[1]Guangdong Laboratory for Lingnan Modern Agriculture,State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources,Key Laboratory of Plant Molecular Breeding of Guangdong Province,College of Agriculture,South China Agricultural University,Guangzhou 510642,China [2]Key Laboratory of Molecular Epigenetics of the Ministry of Education(MOE),Northeast Normal University,Changchun 130024,China [3]Department of Plant and Environmental Sciences,Weizmann Institute of Science,Rehovot 76100,Israel [4]State Key Laboratory of Plant Genomics and National Center for Plant Gene Research,Institute of Genetics and Developmental Biology,Innovation Academy for Seed Design,Chinese Academy of Sciences,Beijing 100101,China [5]These authors contributed equally to this article

出　　处：《Plant Communications》2024年第11期144-156,共13页植物通讯（英文）

基　　金：Double first-class discipline promotion project(2021B10564001);Laboratory of Lingnan Modern Agriculture Project(NT2021001 and NG2021004).

摘　　要：N^(6)-methyladenosine (m^(6)A) is a prevalent internal post-transcriptional modification in eukaryotic RNAs executed by m^(6)A-binding proteins known as “readers.” Our previous research demonstrated that the Arabidopsis m^(6)A reader ECT2 positively regulates transcript levels of the proteasome regulator PTRE1 and several 20S proteasome subunits, thereby enhancing 26S proteasome activity. However, mechanism underlying the selective recognition of m^(6)A targets by readers, such as ECT2, remains elusive. In this study, we further demonstrate that ECT2 physically interacts with PTRE1 and several 20S proteasome subunits. This interaction, which occurs on the ribosome, involves the N terminus of PTRE1, suggesting that ECT2 might bind to the nascent PTRE1 polypeptide. Deleting ECT2’s protein interaction domain impairs its mRNA-binding ability, whereas mutations in the m^(6)A-RNA-binding site do not affect protein-protein interactions. Moreover, introducing a novel protein-binding domain into ECT2 increases transcript levels of proteins interacting with this domain. Our findings indicate that interaction with the PTRE1 protein enhances ECT2’s binding to PTRE1 m^(6)A mRNAs during translation, thereby regulating PTRE1 mRNA levels.

关 键 词：ECT2 20S proteasome m^(6)A RNA protein interaction ARABIDOPSIS 

分 类 号：Q94[生物学—植物学]