Functional relationship of GUN1 and FUG1 in plastid proteostasis
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA509341 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR8310900_1.fastq.gz | Fastqsanger.gz | |||
| SRR8310900_2.fastq.gz | Fastqsanger.gz | |||
| SRR8310901_1.fastq.gz | Fastqsanger.gz | |||
| SRR8310901_2.fastq.gz | Fastqsanger.gz | |||
| SRR8310892_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 24 |
Similar Datasets
Project description:GUN1 integrates retrograde signals in the chloroplast but the underlying mechanism is elusive. FUG1, a chloroplast translation initiation factor, and GUN1 are co-expressed at the transcript level, and FUG1 co-immunoprecipitates with GUN1. We used mutants of GUN1 (gun1-103) and FUG1 (fug1-3) to analyse their functional relationship at the physiological and systems-wide level, the latter including transcriptome and proteome analyses. Absence of GUN1 aggravates the effects of decreased FUG1 levels on chloroplast protein translation, resulting in transient additive phenotypes with respect to photosynthesis, leaf coloration, growth and cold acclimation. Variegation of the var2 mutant is enhanced by gun1-103 in terms of increasing the fraction of white sectors, in contrast to fug1-3 that acts as suppressor. The transcriptomes of fug1-3 and gun1-103 are very similar, but absence of GUN1 alone has almost no effects on protein levels, whereas chloroplast protein accumulation is markedly decreased in fug1-3. In gun1 fug1 double mutants, effects on transcriptomes and particularly proteomes are enhanced. Our results show that GUN1 function becomes critical when chloroplast proteostasis is perturbed by decreased translation (fug1) or degradation (var2) of chloroplast proteins. The functions of FUG1 and GUN1 appear to be related, corroborating the view that GUN1 operates in chloroplast proteostasis.
2019-04-23 | GSE123583 | GEO
Project description:We have previously identified the chloroplast translation initiation factor IF-2, or FUG1, as a GUN1 interactor based on co-immunoprecipitation and co-expression analysis (Tadini et al., 2016). To further investigate the functional relationship between these two proteins, the double mutant gun1-103 fug1-3 was generated by crossing the single gun1-103 knock-out mutant and the fug1-3 knock-down mutant. We performed comparative proteomics on gun1-103 and fug1-3, as well as on the double mutant gun1-103 fug1-3.
2019-06-26 | PXD012067 | Pride
Project description:Functional relationship of Arabidopsis thaliana GUN1 and FUG1 in plastid proteostasis
2020-04-17 | E-GEOD-123583 | ExpressionAtlas
Project description:Plastid gene expression (PGE) acts as a signal that regulates the expression of photosynthesis-associated nuclear genes (PhANGs) via GENOMES UNCOUPLED1 (GUN1)-dependent retrograde signaling. We recently isolated Arabidopsis sugar-inducible cotyledon yellow-192 (sicy-192), a gain-of-function mutant of plastidic invertase (INV-E), and showed that following the treatment of this mutant with sucrose, the expression of PhANGs decreased while that of nitrate reductase 1 (NIA1) increased. Plastid-encoded RNA polymerase (PEP)-dependent PGE was markedly suppressed in the sicy-192 mutant by the sucrose treatment. A double mutant of sicy-192 and gun1-101, a null mutant of GUN1, revealed that metabolic perturbation in the sucrose-treated sicy-192 mutant was, at least in part, dependent on GUN1. To confirm whether there is a relationship between plastid sugar metabolism and nuclear gene expression, we performed a microarray analysis using Suc-treated 3 genotypes consisting of wild-type, sicy-192, and sicy-192 gun1-101 plants.
2013-09-14 | GSE50857 | GEO
Project description:Plastid gene expression (PGE) acts as a signal that regulates the expression of photosynthesis-associated nuclear genes (PhANGs) via GENOMES UNCOUPLED1 (GUN1)-dependent retrograde signaling. We recently isolated Arabidopsis sugar-inducible cotyledon yellow-192 (sicy-192), a gain-of-function mutant of plastidic invertase (INV-E), and showed that following the treatment of this mutant with sucrose, the expression of PhANGs decreased while that of nitrate reductase 1 (NIA1) increased. Plastid-encoded RNA polymerase (PEP)-dependent PGE was markedly suppressed in the sicy-192 mutant by the sucrose treatment. A double mutant of sicy-192 and gun1-101, a null mutant of GUN1, revealed that metabolic perturbation in the sucrose-treated sicy-192 mutant was, at least in part, dependent on GUN1. To confirm whether there is a relationship between plastid sugar metabolism and nuclear gene expression, we performed a microarray analysis using Suc-treated 3 genotypes consisting of wild-type, sicy-192, and sicy-192 gun1-101 plants. Wild-type, sicy-192, and sicy-192 gun1-101 plants were grown on MS medium containing 100 mM sucrose in a growth chamber kept at 25°C during 16 h of light (100 µmol/m2/s) and at 22°C during 8 h of darkness for 4 days. At 4 days of age, cotyledons were collected as samples for microarray analysis.
2013-09-14 | E-GEOD-50857 | biostudies-arrayexpress
Project description:Investigation of the function of GUN1 in the chloroplast (post)-transcriptome We performed gene expression profiling analysis using data obtained from lncRNA-seq of gun1 seedlings with white, marble or green cotyledons
2024-09-12 | GSE247732 | GEO
Project description:Series of 8 repetitions of hybridization of treatment (gun1) and control (WT) each. Comparison of Arabidopsis gun1-1 mutant defective in plastid signaling (protein unknown) versus WT. R.E. Susek et al., Cell 74 (1993), pp. 787-799 Keywords: repeat sample
2005-01-01 | GSE1185 | GEO
Project description:Series of 8 repetitions of hybridization of treatment (gun1) and control (WT) each. Comparison of Arabidopsis gun1-1 mutant defective in plastid signaling (protein unknown) versus WT. R.E. Susek et al., Cell 74 (1993), pp. 787-799 Keywords: repeat sample
2004-12-31 | E-GEOD-1185 | biostudies-arrayexpress
Project description:Photo-inhibitory high-light stress induces damage to photosystems and changes a myriad of metabolic processes in plants. In Arabidopsis it leads to increased abundance of markers of protein degradation and transcriptional upregulation of proteases and proteolytic machinery, but proteostasis is largely maintained. To identify specific enzymes degrading at a faster rate under high light conditions, we developed a 13C partial labelling approach to measure rates of turnover of specific proteins in Arabidopsis rosettes. We identified 73 proteins with rates of protein degradation enhanced by high-light. In addition to the expected increase in degradation rate of the photosystem II (PSII) D1 subunit, we discovered significant increases in degradation rate for specific molecular chaperones, nitrate reductase, glyceraldehyde-3 phosphate dehydrogenase, and phosphoglycerate kinase. Significant increases in degradation of 65 other plastid, mitochondrial, peroxisomal, and cytosolic enzymes were also found, including factors involved in redox shuttles within and between organelles and the cytosol. Coupled analysis of protein degradation rate, transcriptional rate, and protein abundance revealed that 57% of the nuclear-encoded enzymes with higher degradation rates also had high light-induced transcriptional responses, ensuring proteostasis. In contrast, plastid-encoded proteins with enhanced turnover rates showed decreased transcript abundances and must maintain protein abundance by other processes. This analysis reveals a light-induced transcriptional program for nuclear-encoded genes, beyond the regulation of PSII D1 subunit and the function of PSII, to replace key protein degradation targets in plants and ensure proteostasis under high-light stress.
2022-01-19 | GSE131545 | GEO
Project description:The unfolded protein response (UPR) maintains endoplasmic reticulum (ER) proteostasis through the activation of transcription factors such as XBP1s and ATF6. The functional consequences of these transcription factors for ER proteostasis remain poorly defined. Here, we describe methodology that enables orthogonal, small molecule-mediated activation of the UPR-associated transcription factors XBP1s and/or ATF6 in the same cell independent of stress. We employ transcriptomics and quantitative proteomics to evaluate ER proteostasis network remodeling owing to the XBP1s and/or ATF6 transcriptional programs. Furthermore, we demonstrate that the three ER proteostasis environments accessible by activating XBP1s and/or ATF6 differentially influence the folding, trafficking, and degradation of destabilized ER client proteins without globally affecting the endogenous proteome. Our data reveal how the ER proteostasis network is remodeled by the XBP1s and/or ATF6 transcriptional programs at the molecular level and demonstrate the potential for selectively restoring aberrant ER proteostasis of pathologic, destabilized proteins through arm-selective UPR-activation. The unfolded protein response adapts endoplasmic reticulum (ER) proteostasis via stress-responsive transcription factors including XBP1s and ATF6. Here, R. Luke Wiseman and colleagues implement technology for the orthogonal, ligand-dependent activation of XBP1s and/or ATF6 in a single cell. They characterize how XBP1s and/or ATF6 activation impacts ER proteostasis pathway composition and function. Adapted ER environments influence the proteostasis of destabilized protein variants without affecting the endogenous proteome. The work informs the development of proteostasis environment-adapting therapeutics for protein misfolding-related diseases. In order to activate both XBP1s and ATF6 in the same cell, we incorporated DHFR.ATF6 and tet-inducible XBP1s into a HEK293T-REx cell line stably expressing the tet-repressor. The HEK293DYG control cell line expresses tet-inducible eGFP and DHFR.YFP and is used as a control to demonstrate that the addition of doxycycline (dox) and trimethoprim (TMP) do not induce UPR genes. HEK293DYG cells were treated for 12 h with vehicle or 1 μg/mL dox and 10 μM TMP in biological triplicate. Cells were harvested and RNA was extracted using the RNeasy Mini Kit (Qiagen). Genomic DNA was removed by on-column digestion using the RNase-free DNase Set (Qiagen). Data from HEK293DYG cells showed no significant overlap in the ligand-treated transcriptomes obtained from HEK293DAX cells.
2013-04-23 | E-GEOD-44950 | biostudies-arrayexpress