Light-induced LLPS of the CRY2/SPA1/FIO1 complex regulating mRNA methylation and chlorophyll homeostasis in Arabidopsis
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA943418 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR23816900_1.fastq.gz | Fastqsanger.gz | |||
| SRR23816900_2.fastq.gz | Fastqsanger.gz | |||
| SRR23816901_1.fastq.gz | Fastqsanger.gz | |||
| SRR23816901_2.fastq.gz | Fastqsanger.gz | |||
| SRR23816902_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 176 |
Similar Datasets
Project description:Light regulates chlorophyll homeostasis and photosynthesis via various molecular mechanisms in plants. The light regulation of transcription and protein stability of nuclear-encoded chloroplast proteins have been extensively studied, but how light regulation of mRNA metabolism affects abundance of nuclear-encoded chloroplast proteins and chlorophyll homeostasis remains poorly understood. Here we show that the blue light receptor cryptochrome 2 (CRY2) and the METTL16-type m6A writer FIONA1 (FIO1) regulate chlorophyll homeostasis in response to blue light. In contrast to the CRY2-mediated photo-condensation of the mRNA adenosine methylase (MTA), photoexcited CRY2 co-condenses FIO1 only in the presence of the CRY2-signalling protein SUPPRESSOR of PHYTOCHROME A (SPA1). CRY2 and SPA1 synergistically or additively activate the RNA methyltransferase activity of FIO1 in vitro, whereas CRY2 and FIO1, but not MTA, are required for the light-induced methylation and translation of the mRNAs encoding multiple chlorophyll homeostasis regulators in vivo. Our study demonstrates that the light-induced liquid-liquid phase separation of the photoreceptor/writer complexes is commonly involved in the regulation of photoresponsive changes of mRNA methylation, whereas the different photo-condensation mechanisms of the CRY/FIO1 and CRY/MTA complexes explain, at least partially, the writer-specific functions in plant photomorphogenesis.
2023-11-30 | GSE227150 | GEO
Project description:Light modulates expression of nuclear-encoded chloroplast proteins to promote chlorophyll biosynthesis and photosynthesis in plants. Photoregulatory mechanisms regulating transcription and protein stability of nuclear-encoded chloroplast proteins have been extensively studied, but how photoresponsive mRNA metabolism affecting chloroplast proteins remains not well understood. We performed a systematic analysis of the photoresponsive transcriptomes, m6A epitranscriptomes, translatomes, and proteomes in Arabidopsis, leading to a hypothesis that the blue light receptor cryptochromes activate the RNA methyltransferase, FIONA 1 (FIO1), to increase RNA methylation, translation of the nuclear-encoded chlorophyll synthesis enzymes (CSEs), and chlorophyll synthesis. We further demonstrate that the photoresponsive CRY2-interacting protein, SPA1, acts as a chaperone to mediate co-condensation of the CRY2/FIO1 complex, activating the FIO1 methyltransferase activity. This finding demonstrates a previously unknown photoregulatory mechanism controlling chlorophyll biosynthesis in plants.
2024-01-26 | PXD040660 | Pride
Project description:Cryptochromes are blue-light receptors in plants and animals. Homodimers are the physiologically active form of plant cryptochromes that mediates blue light regulation of gene expression and photomorphogenesis, but how light regulates the photoreceptor activation and inactivation remains unclear. We identified an Arabidopsis protein BIC1 (Blue-light Inhibitor of Cryptochromes 1) that inhibits all photoreactions of plant cryptochrome 2 (CRY2) examined, allowing direct tests of the photoactivation and inactivation mechanisms of CRY2. We found that blue light stimulates homodimerization of CRY2, whereas BIC1 binds to CRY2 to suppress CRY2 dimerization and the interaction of CRY2 with its signaling partners. We further show that cryptochromes and phytochromes mediate light induction of BIC1 transcription, evoking the negative feedback circuitry to control homeostasis of the active cryptochromes under the broad spectra of solar radiation in nature.
2016-12-02 | GSE80350 | GEO
Project description:Light is a crucial exogenous signal sensed by cryptochrome (CRY) blue light receptors to modulate growth and the circadian clock in plants and animals. However, how CRYs interpret light quantity to regulate growth in plants remains poorly understood. Furthermore, CRY2 protein levels and activity are tightly regulated in light to fine-tune hypocotyl growth; however, details of the mechanisms that explain precise control of CRY2 levels are not fully understood. We show that in Arabidopsis, UBP12 and UBP13 deubiquitinases physically interact with CRY2 in light. UBP12/13 negatively regulates CRY2 by promoting its ubiquitination and turnover to modulate hypocotyl growth. Growth and development were explicitly affected in blue light when UBP12/13 were disrupted or overexpressed, indicating their role alongside CRY2. UBP12/13 also interacted with and stabilized COP1, which is partially required for CRY2 turnover. Our combined genetic and molecular data support a mechanistic model in which UBP12/13 interact with CRY2 and COP1, leading to the stabilization of COP1. Stabilized COP1 then promotes the ubiquitination and degradation of CRY2 under blue light. Despite decades of studies on deubiquitinases, the knowledge of how their activity is regulated is limited. Our study provides insight into how exogenous signals and ligands, along with their receptors, regulate deubiquitinase activity by protein-protein interaction. Collectively, our results provide a framework of cryptochromes and deubiquitinases to detect and interpret light signals to control plant growth at the most appropriate time.
2022-06-13 | GSE201685 | GEO
Project description:IP mass spectrometry of Arabidopsis CRY2 in dark and blue light
2022-06-09 | PXD032848 | Pride
Project description:Light regulates chlorophyll homeostasis and photosynthesis via various molecular mechanisms in plants. The light regulation of transcription and protein stability of nuclear-encoded chloroplast proteins have been extensively studied, but how light regulation of mRNA metabolism affects abundance of nuclear-encoded chloroplast proteins and chlorophyll homeostasis remains poorly understood. Here we show that the blue light receptor cryptochrome 2 (CRY2) and the METTL16-type m6A writer FIONA1 (FIO1) regulate chlorophyll homeostasis in response to blue light. In contrast to the CRY2-mediated photo-condensation of the mRNA adenosine methylase (MTA), photoexcited CRY2 co-condenses FIO1 only in the presence of the CRY2-signalling protein SUPPRESSOR of PHYTOCHROME A (SPA1). CRY2 and SPA1 synergistically or additively activate the RNA methyltransferase activity of FIO1 in vitro, whereas CRY2 and FIO1, but not MTA, are required for the light-induced methylation and translation of the mRNAs encoding multiple chlorophyll homeostasis regulators in vivo. Our study demonstrates that the light-induced liquid-liquid phase separation of the photoreceptor/writer complexes is commonly involved in the regulation of photoresponsive changes of mRNA methylation, whereas the different photo-condensation mechanisms of the CRY/FIO1 and CRY/MTA complexes explain, at least partially, the writer-specific functions in plant photomorphogenesis.
| S-EPMC10724061 | biostudies-literature
Project description:This sequencing was designed to identify the downstream genes that were regulated by CRY2 in darkness and blue light or regulated by FL1/FL3 in darkness.
2025-05-19 | GSE260607 | GEO
Project description:Potato, S. tuberosum, is one of the most important global crops, but has high levels of waste due to tuber greening under light, which is associated with the accumulation of neurotoxic glycoalkaloids. Here, we have investigated the effect of monochromatic far-red, red, and blue light on the regulation of chlorophyll and glycoalkaloid accumulation in tubers of a commercial variety, King Edward. Transcriptomic analysis of tubers exposed to red, blue, and white light showed that light induction of photosynthesis and tetrapyrrole-related genes grouped into two distinct patterns with one group showing much stronger induction in blue at 6 h and 24 h and a second group showing only red induction at 24 h.
2020-02-25 | E-MTAB-7707 | biostudies-arrayexpress
Project description:CRY2 expression was silenced in MCF7 cells using siRNA oligos, in order to examine the impact of CRY2 knockdown on carcinogenic processes. CRY2 was ~3-fold down-regulated in both replicates, relative to negative control.
2009-01-29 | GSE14617 | GEO
Project description:Small CAB-like proteins (SCPs) are single-helix light-harvesting-like proteins found in all organisms performing oxygenic photosynthesis. We investigated the function of these stress-induced proteins in the cyanobacterium Synechocystis sp. PCC 6803 by comparing a strain, which expresses SCPs constitutively, with a mutant lacking all five SCPs. In the absence of SCPs, cells were larger, and showed irregular thylakoid structure and cell-surfaces. Deletion of scp genes strongly affected the carbon-nitrogen balance, causing accumulation of carbohydrates and a decrease in N-rich compounds (proteins and chlorophyll a). Data from transcriptomic and metabolomic experiments demonstrated that SCPs mediated stabilization of chlorophyll a under stress conditions is crucial to maintain the C/N balance. SCPs diminished the formation of reactive oxygen species, preventing cellular damage by adjusting the de-novo production of chlorophyll a to demand levels. Lack of SCP expression under stress conditions had a large impact on the metabolism of the entire cell. Synechocystis 6803 PSI-less (Shen et al 1993) and PSI-less/ScpABCDE- (Xu et al 2004) mutants were cultivated at 30°C at a light intensity of 4–5 μmol photons m–2 s–1 in BG-11 growth medium (Rippka et al 1979) supplemented with 10 mM glucose. Cells (40–50 ml) from both control and the mutant cultures were collected at mid-log phase by rapid filtration (Pall Supor 800 Filter, 0.8 mm) and total RNA extracted after Pinto et al. (Pinto et al 2009). Single-stranded cDNA preparation, labelling, and hybridization onto the microarray slides were performed after Eisenhut et al. (2007). The microarray slides were scanned with an Agilent Microarray Scanner (model G2505B) with default settings.
2015-03-30 | E-GEOD-59371 | biostudies-arrayexpress