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APIP5 functions as a transcription factor and an RNA-binding protein to modulate cell death and immunity in rice

Many transcription factors (TFs) in animals bind to both DNA and mRNA, regulating transcription and mRNA turnover. However, whether plant TFs function at both the transcriptional and post-transcriptional levels remains unknown. The rice (Oryza sativa) bZIP TF AVRPIZ-T-INTERACTING PROTEIN 5 (APIP5) negatively regulates programmed cell death and blast resistance and is targeted by the effector AvrPiz-t of the blast fungus Magnaporthe oryzae.

Fan ZhangHong Fang , Min WangFeng HeHui TaoRuyi WangJiawei LongJiyang WangGuo-Liang WangYuese Ning

Nucleic Acids Res.; 2022 May 20; 50(9):5064-5079.  doi: 10.1093/nar/gkac316.

Abstract

Many transcription factors (TFs) in animals bind to both DNA and mRNA, regulating transcription and mRNA turnover. However, whether plant TFs function at both the transcriptional and post-transcriptional levels remains unknown. The rice (Oryza sativa) bZIP TF AVRPIZ-T-INTERACTING PROTEIN 5 (APIP5) negatively regulates programmed cell death and blast resistance and is targeted by the effector AvrPiz-t of the blast fungus Magnaporthe oryzae. We demonstrate that the nuclear localization signal of APIP5 is essential for APIP5-mediated suppression of cell death and blast resistance. APIP5 directly targets two genes that positively regulate blast resistance: the cell wall-associated kinase gene OsWAK5 and the cytochrome P450 gene CYP72A1. APIP5 inhibits OsWAK5 expression and thus limits lignin accumulation; moreover, APIP5 inhibits CYP72A1 expression and thus limits reactive oxygen species production and defense compounds accumulation. Remarkably, APIP5 acts as an RNA-binding protein to regulate mRNA turnover of the cell death- and defense-related genes OsLSD1 and OsRac1. Therefore, APIP5 plays dual roles, acting as TF to regulate gene expression in the nucleus and as an RNA-binding protein to regulate mRNA turnover in the cytoplasm, a previously unidentified regulatory mechanism of plant TFs at the transcriptional and post-transcriptional levels.

 

See https://pubmed.ncbi.nlm.nih.gov/35524572/

Figure 2.

Developmental- and pathogen-dependent nuclear accumulation of GFP-APIP5. (A) GFP-APIP5 abundance in cytosolic- and nuclei-enriched fractions from GFP-APIP5 transgenic plants at the seedling and tillering stages. S represents the seedling stage; T represents the tillering stage. Histone H3 served as a nuclear marker and HSP as a cytosolic marker. The experiment was repeated twice (biological replicates) with similar results, and the representative data from one replicate are shown. (B) GFP-APIP5nls abundance in cytosolic- and nuclei-enriched fractions from GFP-APIP5nls transgenic plants at the seedling and tillering stages. S represents the seedling stage; T represents the tillering stage. Histone H3 served as a nuclear marker and HSP as a cytosolic marker. The experiment was repeated twice (biological replicates) with similar results, and the representative data from one replicate are shown. (C) Confocal images showing the subcellular localization of GFP-APIP5 transiently expressed in the leaves of 1- and 2-month-old N. benthamiana plants. mCherry was used a whole-cell localization marker. Scale bars represent 20 μm. (D) GFP-APIP5 abundance in cytosolic- and nuclei-enriched fractions from 1- to 2-month-old N. benthamiana plants. Histone H3 served as a nuclear marker and Actin as a cytosolic marker. The experiment was repeated twice (biological replicates) with similar results, and the representative data from one replicate are shown. (E) GFP-APIP5 abundance in cytosolic- and nuclei-enriched fractions from 3-week-old GFP-APIP5 transgenic plants after inoculation with RO1-1. DAI represents day after inoculation. The experiment was repeated twice (biological replicates) with similar results, and the representative data from one replicate are shown.

 

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