Dimers of the N-terminal domain of phytochrome B are functional in the nucleus
Dimers of the N-terminal domain of phytochrome B are functional in the nucleus
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DOI:
10.1038/nature01837
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发表时间:
2003-07-31
期刊:
影响因子:
64.8
通讯作者:
Nagatani, A
中科院分区:
文献类型:
--
作者:
Matsushita, T;Mochizuki, N;Nagatani, A
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(1). Upon absorption of red light, phytochrome translocates from the cytoplasm to the nucleus(2-4), and regulates gene expression through interaction with transcription factors such as PIF3 (refs 5-7). The phytochrome polypeptide has two domains(1,8) : the amino-terminal photosensory domain with a chromophore and the carboxy-terminal domain which contains signalling motifs such as a kinase domain(9). The latter is widely believed to transduce the signal to downstream components(1,5,810). 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(1), 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.