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Mechanism of early light signaling by the carboxy-terminal output module of Arabidopsis phytochrome B.

Abstract：

:Plant phytochromes are thought to transduce light signals by mediating the degradation of phytochrome-interacting transcription factors (PIFs) through the N-terminal photosensory module, while the C-terminal module, including a histidine kinase-related domain (HKRD), does not participate in signaling. Here we show that the C-terminal module of Arabidopsis phytochrome B (PHYB) is sufficient to mediate the degradation of PIF3 specifically and to activate photosynthetic genes in the dark. The HKRD is a dimerization domain for PHYB homo and heterodimerization. A D1040V mutation, which disrupts the dimerization of HKRD and the interaction between C-terminal module and PIF3, abrogates PHYB nuclear accumulation, photobody biogenesis, and PIF3 degradation. By contrast, disrupting the interaction between PIF3 and PHYB's N-terminal module has little effect on PIF3 degradation. Together, this study demonstrates that the dimeric form of the C-terminal module plays important signaling roles by targeting PHYB to subnuclear photobodies and interacting with PIF3 to trigger its degradation.

journal_name

Nat Commun

journal_title

Nature communications

authors

Qiu Y,Pasoreck EK,Reddy AK,Nagatani A,Ma W,Chory J,Chen M

doi

10.1038/s41467-017-02062-6

subject

Has Abstract

pub_date

2017-12-04 00:00:00

pages

1905

issue

1

issn

2041-1723

pii

10.1038/s41467-017-02062-6

journal_volume

8

pub_type

杂志文章

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