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The Pentatricopeptide Repeat Protein PGR3 Is Required for the Translation of petL and ndhG by Binding Their 5' UTRs.

Authors
  • Higashi, Haruka1
  • Kato, Yoshinobu1
  • Fujita, Tomoya2, 3
  • Iwasaki, Shintaro2, 4, 5
  • Nakamura, Masayuki6
  • Nishimura, Yoshiki1
  • Takenaka, Mizuki1
  • Shikanai, Toshiharu1
  • 1 Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan. , (Japan)
  • 2 RNA Systems Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, 351-0198 Japan. , (Japan)
  • 3 School of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, Yokohama, 226-8503 Japan. , (Japan)
  • 4 Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, 277-8561 Japan. , (Japan)
  • 5 AMED-CREST, Japan Agency for Medical Research and Development, Wako, Saitama 351-0198, Japan. , (Japan)
  • 6 Center of Gene Research, Nagoya University, Nagoya, Aichi, 464-8602 Japan. , (Japan)
Type
Published Article
Journal
Plant and Cell Physiology
Publisher
Oxford University Press
Publication Date
Oct 29, 2021
Volume
62
Issue
7
Pages
1146–1155
Identifiers
DOI: 10.1093/pcp/pcaa180
PMID: 33439244
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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. © The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: [email protected]

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