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

Chan Yul Yoo, Jiangman He, Qing Sang, Yongjian Qiu, Lingyun Long, Ruth Jean-Ae Kim, Emily G. Chong, Joseph Hahm, Nicholas Morffy, Pei Zhou, Lucia C. Strader, Akira Nagatani, Beixin Mo, Xuemei Chen and Meng Chen ()
Additional contact information
Chan Yul Yoo: University of California
Jiangman He: University of California
Qing Sang: University of California
Yongjian Qiu: University of California
Lingyun Long: University of California
Ruth Jean-Ae Kim: University of California
Emily G. Chong: University of California
Joseph Hahm: University of California
Nicholas Morffy: Duke University
Pei Zhou: Duke University School of Medicine
Lucia C. Strader: Duke University
Akira Nagatani: Kyoto University
Beixin Mo: Shenzhen University
Xuemei Chen: University of California
Meng Chen: University of California

Nature Communications, 2021, vol. 12, issue 1, 1-16

Abstract: Abstract 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.

Date: 2021
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-25909-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25909-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-25909-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().