A six‐repeat PPR protein WPR directly binds target RNAs and coordinates chloroplast RNA processing via dual recruitment of MORF1 , MORF8b , and CAF2 proteins in rice

RNA结合蛋白 核糖核酸 五三肽重复 RNA剪接 生物 RNA编辑 内含子 拟南芥 遗传学 细胞生物学 基因 突变体
作者
Bo Zhao,Guojuan Xu,Yajun Zhu,Hui Zhang,Yuanbo Zhang,Chunxue Wei,Xi Chen,Zhichao Wu,Ruifang Liu,Kai Chen,Congcong Shen,Ling Ding,Wang Xu,Wenhui Jiang,W. Frank An,Fangqin Cheng,Xu Zhan,Jianlong Xu,Yong Xiang
出处
期刊:Plant Journal [Wiley]
卷期号:124 (2): e70526-e70526
标识
DOI:10.1111/tpj.70526
摘要

SUMMARY Pentatricopeptide repeat (PPR) proteins are key regulators of organelle RNA metabolism in plants, yet their precise mechanisms in chloroplast RNA processing remain unclear. Here, we identify WPR, a unique P‐type PPR protein in rice ( Oryza sativa L.), as a critical factor in chloroplast RNA splicing and editing. A ~112‐kb chromosomal inversion upstream of WPR causes an albino panicle rachis phenotype ( wpr mutant), while complete loss of WPR function leads to seedling lethality. WPR deficiency disrupts the splicing of multiple group II introns (atpF, ndhA, ndhB, petB, rpl2, and rps12) and impairs RNA editing in transcripts such as ndhA, ndhB, ndhG, rps14, and ycf3. Electrophoretic mobility shift assay (EMSA) data confirm that WPR directly binds to precursor mRNAs of atpF, ndhA, petB, rpl2, and rps12. Strikingly, WPR interacts with both RNA editing factors (MORF1, MORF8b) and the splicing factor CAF2, but not with other PPR proteins targeting the same transcripts. Unlike most PPR proteins, WPR contains only six PPR repeats, which is the fewest among all functionally characterized rice PPR proteins. With few informative repeats, WPR likely possesses a broad, low‐specificity RNA‐binding activity. Moreover, WPR may act on chloroplast RNA maturation by recruiting MORFs and CAF2 rather than other PPR proteins, highlighting a novel regulatory mode in which P‐type PPR protein may act as an RNA‐binding scaffold to integrate diverse RNA‐processing machineries. This study advances the understanding of PPR protein diversity and provides new insights into the molecular mechanisms of chloroplast RNA processing in rice.
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