SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana

Ari Sadanandom, E. Ádám, Beatriz Orosa, András Viczián, Cornelia Klose, Cunjin Zhang, Eve Marie Josse, L. Kozma-Bognár, Ferenc Nagy

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The red/far red light absorbing photoreceptor phytochrome-B (phyB) cycles between the biologically inactive (Pr, λmax, 660 nm) and active (Pfr; λmax, 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 phyBLys996Arg-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.

Original languageEnglish
Pages (from-to)11108-11113
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number35
DOIs
Publication statusPublished - Sep 1 2015

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Phytochrome B
Sumoylation
Arabidopsis
Light
Phytochrome
Ubiquitin
Genetically Modified Plants
Photoperiod

Keywords

  • Photomorphogenesis
  • Photoreceptor
  • Phytochrome
  • Signaling
  • Sumoylation

ASJC Scopus subject areas

  • General

Cite this

SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana. / Sadanandom, Ari; Ádám, E.; Orosa, Beatriz; Viczián, András; Klose, Cornelia; Zhang, Cunjin; Josse, Eve Marie; Kozma-Bognár, L.; Nagy, Ferenc.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 112, No. 35, 01.09.2015, p. 11108-11113.

Research output: Contribution to journalArticle

Sadanandom, Ari ; Ádám, E. ; Orosa, Beatriz ; Viczián, András ; Klose, Cornelia ; Zhang, Cunjin ; Josse, Eve Marie ; Kozma-Bognár, L. ; Nagy, Ferenc. / SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana. In: Proceedings of the National Academy of Sciences of the United States of America. 2015 ; Vol. 112, No. 35. pp. 11108-11113.
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AU - Sadanandom, Ari

AU - Ádám, E.

AU - Orosa, Beatriz

AU - Viczián, András

AU - Klose, Cornelia

AU - Zhang, Cunjin

AU - Josse, Eve Marie

AU - Kozma-Bognár, L.

AU - Nagy, Ferenc

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AB - The red/far red light absorbing photoreceptor phytochrome-B (phyB) cycles between the biologically inactive (Pr, λmax, 660 nm) and active (Pfr; λmax, 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 phyBLys996Arg-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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KW - Signaling

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