Physcomitrium patens pentatricopeptide repeat protein PpPPR_32 is involved in the accumulation of psaC mRNA encoding the iron sulfur protein of photosystem I.
Physcomitrium patens pentatricopeptide repeat protein PpPPR_32 is involved in the accumulation of psaC mRNA encoding the iron sulfur protein of photosystem I.
复制标题
立碗藓五肽重复蛋白 PpPPR_32 参与编码光系统 I 铁硫蛋白的 psaC mRNA 的积累。
DOI：
10.1111/gtc.12928
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发表时间：
2022
期刊：
影响因子：
2.1
通讯作者：
Sugita Mamoru
中科院分区：
文献类型：
--
作者：
Suzuki Ryo;Sugita Chieko;Aoki Setsuyuki;Sugita Mamoru
五肽重复序列（PPR）蛋白参与RNA代谢，并在植物细胞器基因表达的转录后调控中发挥作用。尽管立碗藓中存在上百种PPR蛋白，但其功能尚不完全清楚。在这里，我们报告了P-类PPR蛋白PpPPR_32在P中的功能。patens。利用绿色荧光蛋白进行瞬时表达分析，结果表明PpPPR_32的N-末端具有叶绿体转运肽的功能，表明PpPPR_32定位于叶绿体中; PpPPR_32基因敲除突变体能自养生长，但原丝体生长减少，光系统I（PSI）复合物的形成能力较差。定量真实的实时逆转录聚合酶链反应和RNA凝胶印迹杂交分析显示，编码PSI铁硫蛋白的psaC基因的转录水平显著降低，但其他PSI基因的转录水平没有改变。这表明PpPPR_32特异性地参与psaC基因的表达水平。我们的研究结果表明PpPPR_32对psaCtranscript和PSI复合物的积累是必不可少的。
Pentatricopeptide repeat (PPR) proteins are involved in RNA metabolism and also play a role in posttranscriptional regulation during plant organellar gene expression. Although a hundred of PPR proteins exist in the mossPhyscomitrium patens, their functions are not fully understood. Here, we report the function of P‐class PPR protein PpPPR_32 inP. patens. A transient expression assay using green fluorescent protein demonstrated that the N‐terminal region of PpPPR_32 functions as a chloroplast‐targeting transit peptide, indicating that PpPPR_32 is localized in chloroplasts.PpPPR_32knockout mutants grew autotrophically but with reduced protonema growth and the poor formation of photosystem I (PSI) complexes. Quantitative real‐time reverse transcription‐polymerase chain reaction and RNA gel blot hybridization analyses revealed a significant reduction in the transcript level of thepsaCgene encoding the iron sulfur protein of PSI but no alteration to the transcript levels of other PSI genes. This suggests that PpPPR_32 is specifically involved in the expression level of thepsaCgene. Our results indicate that PpPPR_32 is essential for the accumulation ofpsaCtranscript and PSI complexes.