<i>Arabidopsis</i> Phytochrome A Is Modularly Structured to Integrate the Multiple Features That Are Required for a Highly Sensitized Phytochrome

Oka, Yoshitomo; Ono, Yuya; Toledo‐Ortiz, Gabriela; Kokaji, Keio; Matsui, Minami; Mochizuki, Naoki; Nagatani, Akira

doi:10.1105/tpc.111.094201

Cited by 20 publications

(19 citation statements)

References 102 publications

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“…In addition, a truncated Arabidopsis phyA N-terminal mutant (PHYA686-YEP-DD) was imported into the nucleus and degraded under red light, even though its degradation was a little slower than that of wild-type PHYA-YEP; however, PHYA686-YEP-DD did not initiate far-red HIR signalling responses (25). Moreover, studies with chimeric phytochromes between Arabidopsis PHYA and PHYB confirmed that the 415 N-terminal amino acid (N-PAS and GAF domain) of Arabidopsis phy A is critical for rapid Pfr phyA degradation (32).…”

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confidence: 60%

“…N-terminal domain of phyA is important for the biological activities of phytochrome A (32,42). Some point mutations in the N-terminal domain of phyA adversely affect the biological functions of phyA (43).…”

Section: Discussionmentioning

confidence: 99%

“…Lysine 206 of Arabidopsis phyA is the main ubiquitination site The N-terminal domain of phyA has been shown to be ubiquitinated and degraded as a result of the biochemical response to light (31,32). Identification of ubiquitination site can be accomplished by either direct analysis of ubiquitinated proteins by mass spectrometry (MS) or protein degradation analysis using lysine mutated proteins (34,35).…”

Section: Resultsmentioning

confidence: 99%

“…To define specific ubiquinated lysines in phyA, C-terminal conserved lysines within the region required for Pfr signal transduction of oat phyA were replaced with arginines but these mutant phyA proteins showed the same degradation kinetics as wild-type phyA (31). Recent phyA functional studies showed that the N-terminal domain of phyA is important for ubiquitination and degradation (25,31,32). We identified lysines in the N-terminal of phyA involved in ubiquitination and degradation.…”

Section: Discussionmentioning

confidence: 99%

“…Previous phyA degradation studies (31,32) found that the N-terminal domain of phyA plays an important role in phyA degradation, with some contribution from the C-terminal domain. The N-terminal domain of potato phyA is required for phyA degradation through the selective recognition and ubiquitination of Pfr function (31).…”

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confidence: 99%

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Lysine 206 inArabidopsisphytochrome A is the major site for ubiquitin-dependent protein degradation

2015

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confidence: 60%

Section: Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Lysine 206 inArabidopsisphytochrome A is the major site for ubiquitin-dependent protein degradation

2015

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A de novo transcriptome analysis revealed that photomorphogenic genes are required for carotenoid synthesis in the dark-grown carrot taproot

et al. 2020

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Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis

et al. 2017

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The switch from skotomorphogenesis to photomorphogenesis is a key developmental transition in the life of seed plants. While much of the underpinning proteome remodeling is driven by light-induced changes in gene expression, the proteolytic removal of specific proteins by the ubiquitin-26S proteasome system is also likely paramount. Through mass spectrometric analysis of ubiquitylated proteins affinity-purified from etiolated Arabidopsis seedlings before and after red-light irradiation, we identified a number of influential proteins whose ubiquitylation status is modified during this switch. We observed a substantial enrichment for proteins involved in auxin, abscisic acid, ethylene, and brassinosteroid signaling, peroxisome function, disease resistance, protein phosphorylation and light perception, including the phytochrome (Phy) A and phototropin photoreceptors. Soon after red-light treatment, PhyA becomes the dominant ubiquitylated species, with ubiquitin attachment sites mapped to six lysines. A PhyA mutant protected from ubiquitin addition at these sites is substantially more stable in planta upon photoconversion to Pfr and is hyperactive in driving photomorphogenesis. However, light still stimulates ubiquitylation and degradation of this mutant, implying that other attachment sites and/or proteolytic pathways exist. Collectively, we expand the catalog of ubiquitylation targets in Arabidopsis and show that this post-translational modification is central to the rewiring of plants for photoautotrophic growth.

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Arabidopsis Phytochrome A Is Modularly Structured to Integrate the Multiple Features That Are Required for a Highly Sensitized Phytochrome

Cited by 20 publications

References 102 publications

Lysine 206 inArabidopsisphytochrome A is the major site for ubiquitin-dependent protein degradation

Lysine 206 inArabidopsisphytochrome A is the major site for ubiquitin-dependent protein degradation

A de novo transcriptome analysis revealed that photomorphogenic genes are required for carotenoid synthesis in the dark-grown carrot taproot

Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis

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