bims-plasge 2021-04-25 papers

Issue of 2021–04–25
two papers selected by
Vera S. Bogdanova, ИЦиГ СО РАН

Plant Physiol. 2019 Nov 04. 181(3): 891-900

Establishment of a Heterologous RNA Editing Event in Chloroplasts1 [OPEN].

Filomena Vanessa Loiacono, Wolfram Thiele, Mark Aurel Schöttler, Michael Tillich, Ralph Bock.

In chloroplasts and plant mitochondria, specific cytidines in mRNAs are posttranscriptionally converted to uridines by RNA editing. Editing sites are recognized by nucleus-encoded RNA-binding proteins of the pentatricopeptide repeat (PPR) family, which bind upstream of the editing site in a sequence-specific manner and direct the editing activity to the target position. Editing sites have been lost many times during evolution by C-to-T mutations. Loss of an editing site is thought to be accompanied by loss or degeneration of its cognate PPR protein. Consequently, foreign editing sites are usually not recognized when introduced into species lacking the site. Previously, the spinach (Spinacia oleracea) psbF-26 editing site was introduced into the tobacco (Nicotiana tabacum) plastid genome. Tobacco lacks the psbF-26 site and cannot edit it. Expression of the "unedited" PsbF protein resulted in impaired PSII function. In Arabidopsis (Arabidopsis thaliana), the PPR protein LPA66 is required for editing at psbF-26. Here, we show that introduction of the Arabidopsis LPA66 reconstitutes editing of the spinach psbF-26 site in tobacco and restores a wild-type-like phenotype. Our findings define the minimum requirements for establishing new RNA editing sites and suggest that the evolutionary dynamics of editing patterns is largely explained by coevolution of editing sites and PPR proteins.

DOI: https://doi.org/10.1104/pp.19.00922

Plant Physiol. 2019 Aug 29. 181(1): 55-62

WRINKLED1 Regulates BIOTIN ATTACHMENT DOMAIN-CONTAINING Proteins that Inhibit Fatty Acid Synthesis1[OPEN].

Hui Liu, Zhiyang Zhai, Kate Kuczynski, Jantana Keereetaweep, Jorg Schwender, John Shanklin.

WRINKLED1 (WRI1) is a transcriptional activator that binds to a conserved sequence (designated as AW box) boxes in the promoters of many genes from central metabolism and fatty acid (FA) synthesis, resulting in their transcription. BIOTIN ATTACHMENT DOMAIN-CONTAINING (BADC) proteins lack a biotin-attachment domain and are therefore inactive, but in the presence of excess FA, BADC1 and BADC3 are primarily responsible for the observed long-term irreversible inhibition of ACETYL-COA CARBOXYLASE, and consequently FA synthesis. Here, we tested the interaction of WRI1 with BADC genes in Arabidopsis (Arabidopsis thaliana) and found purified WRI1 bound with high affinity to canonical AW boxes from the promoters of all three BADC genes. Consistent with this observation, both expression of BADC1, BADC2, and BADC3 genes and BADC1 protein levels were reduced in wri1-1 relative to the wild type, and elevated upon WRI1 overexpression. The double mutant badc1 badc2 phenocopied wri1-1 with respect to both reduction in root length and elevation of indole-3-acetic acid-Asp levels relative to the wild type. Overexpression of BADC1 in wri1-1 decreased indole-3-acetic acid-Asp content and partially rescued its short-root phenotype, demonstrating a role for BADCs in seedling establishment. That WRI1 positively regulates genes encoding both FA synthesis and BADC proteins (i.e. conditional inhibitors of FA synthesis), represents a coordinated mechanism to achieve lipid homeostasis in which plants couple the transcription of their FA synthetic capacity with their capacity to biochemically downregulate it.

DOI: https://doi.org/10.1104/pp.19.00587