期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 35, 页码 11108-11113出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1415260112
关键词
photoreceptor; phytochrome; sumoylation; signaling; photomorphogenesis
资金
- Biotechnology and Biological Sciences Research Council [BB/K006975/1]
- Hungarian Scientific Research Fund [K-108559, NN-110636]
- Bolyai Janos Scholarship of the Hungarian Academy of Sciences
- Biotechnology and Biological Sciences Research Council
- European Research Council
- BBSRC [BB/K006975/1, BB/M002136/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K006975/1, BB/M002136/1] Funding Source: researchfish
The red/far red light absorbing photoreceptor phytochrome-B (phyB) cycles between the biologically inactive (Pr, lambda(max), 660 nm) and active (Pfr; lambda(max), 730 nm) forms and functions as a light quality and quantity controlled switch to regulate photomorphogenesis in Arabidopsis. At the molecular level, phyB interacts in a conformation-dependent fashion with a battery of downstream regulatory proteins, including PHYTOCHROME INTERACTING FACTOR transcription factors, and by modulating their activity/abundance, it alters expression patterns of genes underlying photomorphogenesis. Here we report that the small ubiquitin-like modifier (SUMO) is conjugated (SUMOylation) to the C terminus of phyB; the accumulation of SUMOylated phyB is enhanced by red light and displays a diurnal pattern in plants grown under light/dark cycles. Our data demonstrate that (i) transgenic plants expressing the mutant phyB(Lys996Arg)-YFP photoreceptor are hypersensitive to red light, (ii) light-induced SUMOylation of the mutant phyB is drastically decreased compared with phyB-YFP, and (iii) SUMOylation of phyB inhibits binding of PHYTOCHROME INTERACTING FACTOR 5 to phyB Pfr. In addition, we show that OVERLY TOLERANT TO SALT 1 (OTS1) de-SUMOylates phyB in vitro, it interacts with phyB in vivo, and the ots1/ots2 mutant is hyposensitive to red light. Taken together, we conclude that SUMOylation of phyB negatively regulates light signaling and it is mediated, at least partly, by the action of OTS SUMO proteases.
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