Fig. 2: PIF3 possesses a p53-like AD. | Nature Communications

Fig. 2: PIF3 possesses a p53-like AD.

From: Direct photoresponsive inhibition of a p53-like transcription activation domain in PIF3 by Arabidopsis phytochrome B

Fig. 2

a Amino acid sequence alignment of the ADs of Homo sapiens p53 (BAC16799.1), Saccharomyces cerevisiae Gcn4 (QHB08060.1), and select PIF3 orthologs from eudicots, including Arabidopsis thaliana (NP_001318964.1), Abrus precatorius (XP_027363600.1), Populus alba (XP_034896271.1), Hevea brasiliensis (XP_021639209.1), Citrus clementina (XP_006423962.1), Vitis riparia (XP_034707239.1), Cannabis sativa (XP_030504594.1), and Quercus lobata (XP_030957900.1). b Amino acid sequence alignment of the AD regions of PIF3, PIF3mAD, and the other PIF paralogs in Arabidopsis. The substituted alanines in PIF3mAD are labeled in orange. a, b The conserved activator ΦxxΦΦ motifs are highlighted in bold; the critical hydrophobic residues in the ΦxxΦΦ motif and the flanking acidic residues are labeled in magenta and blue, respectively. c Yeast transactivation assays showing the transactivation activities of the full-length PIF3 and PIF3 paralogs in Arabidopsis and the respective mAD mutants of PIF3, PIF8, PIF1, PIF5, PIF4, and PIF7. All mAD mutants contain five alanine substitutions in the predicted ΦxxΦΦ motif regions shown in (b). The left panel shows serial dilutions of the yeast strains containing the respective constructs grown on either SD/-Trp/-Leu/+AbA or SD/-Trp/-Leu (control) media. The right panel shows the relative transactivation activities quantified using the yeast liquid β-galactosidase assay. The transactivation activities were calculated relative to that of PIF3. Error bars represent the s.d. of three biological replicates; the centers of the error bars represent the mean values; the numbers represent the mean value of the relative activity. Fold changes in the activity of mAD mutants relative to their respective wild-type proteins are denoted. The statistical significance of the changes between the mAD mutants and their respective wild-type proteins was analyzed by two-tailed Student’s t-test (****P ≤ 0.0001, n.s. indicates no significant difference). The source data underlying the yeast liquid β-galactosidase assays in (c) are provided in the Source data file.

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