文献类型： 外文期刊

作者： Ma, Liqun ¹ ; Yang, Yongfang ¹ ; Wang, Yuqiu ² ; Cheng, Ke ¹ ; Zhou, Xiwen ¹ ; Li, Jinyan ¹ ; Zhang, Jingyu ¹ ; Li, Ran ¹ ; Zhang, Lingling ¹ ; Wang, Keru ¹ ; Zeng, Ni ¹ ; Gong, Yanyan ² ; Zhu, Danmeng ² ; Deng, Zhiping ⁴ ; Qu, Guiqin ¹ ; Zhu, Benzhong ¹ ; Fu, Daqi ¹ ; Luo, Yunbo ¹ ; Zhu, Hongliang ¹ ;

作者机构： 1.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China

2.Peking Univ, Sch Adv Agr Sci, Beijing 100871, Peoples R China

3.Peking Univ, Sch Life Sci, Beijing 100871, Peoples R China

4.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, State Key Lab Managing Biot & Chem Threats Qual &, Hangzhou 310021, Zhejiang, Peoples R China

5.Tsinghua Univ, Tsinghua Peking Joint Ctr Life Sci, Sch Life Sci, MOE Key Lab Bioinformat, Beijing 100084, Peoples R China

6.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China

期刊名称：PLANT CELL （ 影响因子：12.085； 五年影响因子：12.796 ）

ISSN： 1040-4651

年卷期： 2022 年 34 卷 7 期

页码：

收录情况： SCI

摘要： The glycine-rich RNA-binding protein SlRBP1 maintains chloroplast functions via regulating translational efficiency of key transcripts associated with chloroplast function. Many glycine-rich RNA-binding proteins (GR-RBPs) have critical functions in RNA processing and metabolism. Here, we describe a role for the tomato (Solanum lycopersicum) GR-RBP SlRBP1 in regulating mRNA translation. We found that SlRBP1 knockdown mutants (slrbp1) displayed reduced accumulation of total chlorophyll and impaired chloroplast ultrastructure. These phenotypes were accompanied by deregulation of the levels of numerous key transcripts associated with chloroplast functions in slrbp1. Furthermore, native RNA immunoprecipitation-sequencing (nRIP-seq) recovered 61 SlRBP1-associated RNAs, most of which are involved in photosynthesis. SlRBP1 binding to selected target RNAs was validated by nRIP-qPCR. Intriguingly, the accumulation of proteins encoded by SlRBP1-bound transcripts, but not the mRNAs themselves, was reduced in slrbp1 mutants. Polysome profiling followed by RT-qPCR assays indicated that the polysome occupancy of target RNAs was lower in slrbp1 plants than in wild-type. Furthermore, SlRBP1 interacted with the eukaryotic translation initiation factor SleIF4A2. Silencing of SlRBP1 significantly reduced SleIF4A2 binding to SlRBP1-target RNAs. Taking these observations together, we propose that SlRBP1 binds to and channels RNAs onto the SleIF4A2 translation initiation complex and promotes the translation of its target RNAs to regulate chloroplast functions.