Lysine 206 in<i>Arabidopsis</i>phytochrome A is the major site for ubiquitin-dependent protein degradation

Rattanapisit, Kaewta; Cho, Man-Ho; Bhoo, Seong Hee

doi:10.1093/jb/mvv085

Cited by 7 publications

(9 citation statements)

References 44 publications

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“…Nonetheless, our data agree with Rattanapisit et al (2016) that K206 is an influential residue, but also provide a cautionary example that PhyA levels prior to photoexcitation significantly influence the rate of Pfr clearance. We hypothesize that the effect of initial PhyA levels on degradation rate stems from limited capacity in the machinery needed to recognize and ubiquitylate PhyA and is further accentuated by our experimental conditions that used a sharp dark to red-light transition to provoke a rapid influx of Pfr.…”

Section: Discussionsupporting

confidence: 87%

“…Following the completion of this analysis, Rattanapisit et al (2016) reported, using a candidate approach based on amino acid sequence alignments followed by turnover assays of lysine to arginine substitutions, that K206 is critical for PhyA ubiquitylation and degradation as Pfr, but unfortunately, this study did not account for the strong effects of initial PhyA abundance on turnover. Here, we repeated this degradation kinetic using three independent homozygous lines expressing the FLAG-tagged K206-R chromoprotein at levels similar to those of wild-type PhyA and PhyA-FLAG (Supplemental Figure 7A).…”

Section: Resultsmentioning

confidence: 99%

“…We also note that several of our mapped sites have neighboring lysines that could become alternatives (e.g., K95, K202, and K608, and K946; Figure 6B). Rattanapisit et al (2016) investigated the K202 and K206 pair and found that the single K202 chromoprotein was degraded like wild-type PhyA and that the double mutant was no more stable than the K206 variant, suggesting that K202 is not a relevant substitute. They and Clough et al (1999) also tested several other conserved lysines in PhyA (e.g., K165, K284, K286, K400, K739, K744, K784, and K796); none were found to be effective in stabilizing Pfr.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionsupporting

confidence: 87%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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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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“…Rapid light‐dependent degradation is a key feature of phyA that distinguishes phyA from phytochromes having an action peak in R (Sharrock & Clack ). In this regard, the recently described phyA K206R mutant is of special interest (Rattanapisit et al ). Light‐induced degradation of phyA K206R is delayed compared to the wild type, and it will be interesting to measure detailed action spectra for phyA K206R expressing seedlings to verify the prediction that phyA degradation is critical to shape the phyA action spectrum.…”

Section: How To Shift the Phytochrome A Action Peak Towards Far‐red?mentioning

confidence: 99%

Molecular mechanisms and ecological function of far‐red light signalling

Sheerin

Hiltbrunner

2017

Plant Cell & Environment

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Land plants possess the ability to sense and respond to far-red light (700-760 nm), which serves as an important environmental cue. Due to the nature of far-red light, it is not absorbed by chlorophyll and thus is enriched in canopy shade and will also penetrate deeper into soil than other visible wavelengths. Far-red light responses include regulation of seed germination, suppression of hypocotyl growth, induction of flowering and accumulation of anthocyanins, which depend on one member of the phytochrome photoreceptor family, phytochrome A (phyA). Here, we review the current understanding of the underlying molecular mechanisms of how plants sense far-red light through phyA and the physiological responses to this light quality. Light-activated phytochromes act on two primary pathways within the nucleus; suppression of the E3 ubiquitin ligase complex CUL4/DDB1 and inactivation of the PHYTOCHROME INTERACTING FACTOR (PIF) family of bHLH transcription factors. These pathways integrate with other signal transduction pathways, including phytohormones, for tissue and developmental stage specific responses. Unlike other phytochromes that mediate red-light responses, phyA is transported from the cytoplasm to the nucleus in far-red light by the shuttle proteins FAR-RED ELONGATED HYPOCOTYL 1 (FHY1) and FHY1-LIKE (FHL). However, additional mechanisms must exist that shift the action of phyA to far-red light; current hypotheses are discussed.

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“…Data are the mean 6 SE from three independent experiments. a Lys residue corresponding to Lys-206 of At-phyA, which is the main ubiquitination site for its proteasomal degradation (Rattanapisit et al, 2016). The type II-like photostability of Mp-phy suggests that the mechanism for rapid degradation via the ubiquitination of Lys-206 of At-phyA could have been acquired during the course of functional differentiation of phytochromes following gene duplication.…”

Section: Light Stability and Subcellular Distribution Of Mp-phymentioning

confidence: 99%

Phytochrome Signaling Is Mediated by PHYTOCHROME INTERACTING FACTOR in the Liverwort Marchantia polymorpha

et al. 2016

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ORCID ID: 0000-0003-0504-8196 (K. Ishizaki)Phytochromes are red light (R) and far-red light (FR) receptors that play important roles in many aspects of plant growth and development. Phytochromes mainly function in the nucleus and regulate sets of genes by inhibiting negatively acting basic helix-loop-helix transcription factors named PHYTOCHROME INTERACTING FACTORs (PIFs) in Arabidopsis thaliana. Although R/FR photoreversible responses and phytochrome genes are well documented in diverse lineages of plants, the extent to which phytochrome signaling is mediated by gene regulation beyond angiosperms remains largely unclear. Here, we show that the liverwort Marchantia polymorpha, an emerging model basal land plant, has only one phytochrome gene, Mp-PHY, and only one PIF gene, Mp-PIF. These genes mediate typical low fluence responses, which are reversibly elicited by R and FR, and regulate gene expression. Mp-phy is light-stable and translocates into the nucleus upon irradiation with either R or FR, demonstrating that the single phytochrome Mp-phy exhibits combined biochemical and cell-biological characteristics of type I and type II phytochromes. Mp-phy photoreversibly regulates gemma germination and downstream gene expression by interacting with Mp-PIF and targeting it for degradation in an R-dependent manner. Our findings suggest that the molecular mechanisms for light-dependent transcriptional regulation mediated by PIF transcription factors were established early in land plant evolution.

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

Cited by 7 publications

References 44 publications

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

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

Molecular mechanisms and ecological function of far‐red light signalling

Phytochrome Signaling Is Mediated by PHYTOCHROME INTERACTING FACTOR in the Liverwort Marchantia polymorpha

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