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

Photoactivated phytochrome B (PHYB) binds to antagonistically acting PHYTOCHROME-INTERACTING transcription FACTORs (PIFs) to regulate hundreds of light responsive genes in Arabidopsis by promoting PIF degradation. However, whether PHYB directly controls the transactivation activity of PIFs remains a...

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Bibliographic Details
Published in:Nature communications 2021-09, Vol.12 (1), p.5614-5614, Article 5614
Main Authors: Yoo, Chan Yul, He, Jiangman, Sang, Qing, Qiu, Yongjian, Long, Lingyun, Kim, Ruth Jean-Ae, Chong, Emily G., Hahm, Joseph, Morffy, Nicholas, Zhou, Pei, Strader, Lucia C., Nagatani, Akira, Mo, Beixin, Chen, Xuemei, Chen, Meng
Format: Article
Language:English
Subjects:
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Arabidopsis
Control stability
Gene expression
Genes
Humanities and Social Sciences
Hydrophobicity
Kinases
multidisciplinary
p53 Protein
Phytochrome B
Science
Science (multidisciplinary)
Signaling
Transcription activation
Transcription factors
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Summary:Photoactivated phytochrome B (PHYB) binds to antagonistically acting PHYTOCHROME-INTERACTING transcription FACTORs (PIFs) to regulate hundreds of light responsive genes in Arabidopsis by promoting PIF degradation. However, whether PHYB directly controls the transactivation activity of PIFs remains ambiguous. Here we show that the prototypic PIF, PIF3, possesses a p53-like transcription activation domain (AD) consisting of a hydrophobic activator motif flanked by acidic residues. A PIF3mAD mutant, in which the activator motif is replaced with alanines, fails to activate PIF3 target genes in Arabidopsis , validating the functions of the PIF3 AD in vivo. Intriguingly, the N-terminal photosensory module of PHYB binds immediately adjacent to the PIF3 AD to repress PIF3’s transactivation activity, demonstrating a novel PHYB signaling mechanism through direct interference of the transactivation activity of PIF3. Our findings indicate that PHYB, likely also PHYA, controls the stability and activity of PIFs via structurally separable dual signaling mechanisms. Photoactivated phytochrome B regulates gene expression by interacting with PIF transcription factors. Here the authors show that PIF3 contains a p53-like transcription activation domain (AD) and that PHYB can directly suppress PIF3 transactivation activity by binding adjacent to the AD.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-021-25909-5