Rice PPS1 encodes a DYW motif-containing pentatricopeptide repeat protein required for five consecutive RNA-editing sites of nad3 in mitochondria

The New Phytologist
Haijun XiaoJun Hu

Abstract

The pentatricopeptide repeat (PPR) protein family is a large family characterized by tandem arrays of a degenerate 35-amino-acid motif whose members function as important regulators of organelle gene expression at the post-transcriptional level. Despite the roles of PPRs in RNA editing in organelles, their editing activities and the underlying mechanism remain obscure. Here, we show that a novel DYW motif-containing PPR protein, PPS1, is associated with five conserved RNA-editing sites of nad3 located in close proximity to each other in mitochondria, all of which involve conversion from proline to leucine in rice. Both pps1 RNAi and heterozygous plants are characterized by delayed development and partial pollen sterility at vegetative stages and reproductive stage. RNA electrophoresis mobility shift assays (REMSAs) and reciprocal competition assays using different versions of nad3 probes confirm that PPS1 can bind to cis-elements near the five affected sites, which is distinct from the existing mode of PPR-RNA binding because of the continuity of the editing sites. Loss of editing at nad3 in pps1 reduces the activity of several complexes in the mitochondrial electron transport chain and affects mitochondrial morphology. Taken t...Continue Reading

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Citations

May 12, 2019·Plant & Cell Physiology·Zhenjing RenYunjun Liu
Apr 16, 2020·BMC Plant Biology·Weilong YangShaoqing Li
Nov 16, 2019·International Journal of Molecular Sciences·Hong-Gang SuYou-Zhi Ma
May 3, 2020·Molecular Biology Reports·Ahmed M Ramadan
May 14, 2020·International Journal of Molecular Sciences·Cesar Augusto MedinaLong-Xi Yu
Jan 3, 2021·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·Peng ZhengJumin Tu

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