The Pentatricopeptide Repeat Protein PGR3 Is Required for the Translation of petL and ndhG by Binding Their 5′ UTRs
| Autor: | Mizuki Takenaka, Tomoya Fujita, Haruka Higashi, Toshiharu Shikanai, Yoshiki Nishimura, Shintaro Iwasaki, Masayuki Nakamura, Yoshinobu Kato |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Small RNA Physiology Plant Science Biology Ribosome 03 medical and health sciences 0302 clinical medicine Gene Expression Regulation Plant Translational regulation Protein biosynthesis Ribosome profiling Arabidopsis Proteins RNA-Binding Proteins RNA NADH Dehydrogenase Translation (biology) Cell Biology General Medicine Cell biology 030104 developmental biology Amino Acid Substitution Cytochromes b6 Pentatricopeptide repeat 5' Untranslated Regions 030217 neurology & neurosurgery |
| Zdroj: | Plant and Cell Physiology. 62:1146-1155 |
| ISSN: | 1471-9053 0032-0781 |
| DOI: | 10.1093/pcp/pcaa180 |
| Popis: | PGR3 is a P-class pentatricopeptide repeat (PPR) protein required for the stabilization of petL operon RNA and the translation of the petL gene in plastids. Irrespective of its important roles in plastids, key questions have remained unanswered, including how PGR3 protein promotes translation and which plastid mRNA PGR3 activates the translation. Here, we show that PGR3 facilitates the translation from ndhG, in addition to petL, through binding to their 5′ untranslated regions (UTRs). Ribosome profiling and RNA sequencing in pgr3 mutants revealed that translation from petL and ndhG was specifically suppressed. Harnessing small RNA fragments protected by PPR proteins in vivo, we probed the PGR3 recruitment to the 5′ UTRs of petL and ndhG. The putative PGR3-bound RNA segments per se repress the translation possibly with a strong secondary structure and thereby block ribosomes’ access. However, the PGR3 binding antagonizes the effects and facilitates the protein synthesis from petL and ndhG in vitro. The prediction of the 3-dimensional structure of PGR3 suggests that the 26th PPR motif plays important roles in target RNA binding. Our data show the specificity of a plastidic RNA-binding protein and provide a mechanistic insight into translational control. |
| Databáze: | OpenAIRE |
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