Dimers of the N-terminal domain of phytochrome B are functional in the nucleus

Tomonao Matsushita, Nobuyoshi Mochizuki, Akira Nagatani

Research output: Contribution to journalArticle

215 Citations (Scopus)

Abstract

A plant modulates its developmental processes in response to light by several informational photoreceptors such as phytochrome. Phytochrome is a dimeric chromoprotein which regulates various aspects of plant development from seed germination to flowering. Upon absorption of red light, phytochrome translocates from the cytoplasm to the nucleus, and regulates gene expression through interaction with transcription factors such as PIF3 (refs 5-7). The phytochrome polypeptide has two domains: the amino-terminal photosensory domain with a chromophore and the carboxy-terminal domain which contains signalling motifs such as a kinase domain. The latter is widely believed to transduce the signal to downstream components Here we show that the C-terminal domain of Arabidopsis phytochrome B (phyB), which is known as the most important member of the phytochrome family, is not directly involved in signal transduction. The N-terminal domain isolated from phyB, when dimerized and localized in the nucleus, triggered full phyB responses with much higher photosensitivity than the full-length phyB. These findings indicate that the C-terminal domain attenuates the activity of phyB rather than positively transducing the signal.

Original languageEnglish
Pages (from-to)571-574
Number of pages4
JournalNature
Volume424
Issue number6948
DOIs
Publication statusPublished - Jul 31 2003
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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