Arabidopsis thaliana
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA188710 | ENA |
REPOSITORIES: ENA
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Project description:Expression profiling of two-weeks-old wild type, nar1-4/- and nbp35-3/- mutant seedlings. The cytosolic Fe -S cluster assembly pathway is involved in cytosolic and nucleus Fe-S protein maturation. The nar1 mutant was identified by the screeing for abnormal transcription feature in endosperm.We performed genome-wide transcriptional profiling of weak allele nar1-4/- using microarrays to estimate whether the cytosolic Fe -S cluster assembly could affect on the transcriptional profile even in vegetative tissues. Two biological replicate were performed using two weeks seedling of wild type, nar1-4/- and nbp35-3/-. RNA was extracted using the RNeasy mini kit(QIAGEN).
2013-05-01 | E-GEOD-44116 | biostudies-arrayexpress
Project description:Expression profiling of two-weeks-old wild type, nar1-4/- and nbp35-3/- mutant seedlings. The cytosolic Fe -S cluster assembly pathway is involved in cytosolic and nucleus Fe-S protein maturation. The nar1 mutant was identified by the screeing for abnormal transcription feature in endosperm.We performed genome-wide transcriptional profiling of weak allele nar1-4/- using microarrays to estimate whether the cytosolic Fe -S cluster assembly could affect on the transcriptional profile even in vegetative tissues.
2013-05-01 | GSE44116 | GEO
Project description:Proteins incorporating iron-sulfur (Fe-S) cofactors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries located in the cytosol, mitochondria and chloroplasts. After de novo formation on scaffold proteins, Fe-S centers are loaded on client proteins by use of Fe-S cluster transfer proteins. Among plastidial representatives of this latter category, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters found in photosystem I subunits acting upstream of HCF101. NFU2 is additionally required for the maturation of the [2Fe-2S] dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant Arabidopsis thaliana NFU1 is able to solely assemble a [4Fe-4S] cluster per homodimer. We also provide insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins by performing co-immunoprecipitation experiments and assaying the physical interaction of NFU1 with many [4Fe-4S]-containing plastidial proteins using binary yeast two-hybrid assays. Interactions with two proteins involved in isoprenoid and thiamine biosynthesis, respectively 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase (ISPG) and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase (THIC), have been further confirmed by bimolecular fluorescence complementation and in vitro Fe-S cluster transfer experiments. The additional interactions detected with SUFD and SUFA allowed building a model in which NFU1 receives its Fe-S cluster from the SUFBC2D scaffold complex and serves for the maturation of [4Fe-4S] client proteins.
2020-07-06 | PXD015295 | Pride
Project description:Iron–sulfur (Fe–S) clusters play an essential role in plants as protein cofactors mediating diverse electron transfer reactions. Because they can react with oxygen to form reactive oxygen species (ROS) and inflict cellular damage, the biogenesis of Fe–S clusters is highly regulated. A recently discovered group of 2Fe–2S proteins, termed NEET proteins, was proposed to coordinate Fe–S, Fe and ROS homeostasis in mammalian cells. Here we report that disrupting the function of AtNEET, the sole member of the NEET protein family in Arabidopsis thaliana, triggers leaf‐associated Fe–S‐ and Fe‐deficiency responses, elevated Fe content in chloroplasts (1.2–1.5‐fold), chlorosis, structural damage to chloroplasts and a high seedling mortality rate. Our findings suggest that disrupting AtNEET function disrupts the transfer of 2Fe–2S clusters from the chloroplastic 2Fe–2S biogenesis pathway to different cytosolic and chloroplastic Fe–S proteins, as well as to the cytosolic Fe–S biogenesis system, and that uncoupling this process triggers leaf‐associated Fe–S‐ and Fe‐deficiency responses that result in Fe over‐accumulation in chloroplasts and enhanced ROS accumulation. We further show that AtNEET transfers its 2Fe–2S clusters to DRE2, a key protein of the cytosolic Fe–S biogenesis system, and propose that the availability of 2Fe–2S clusters in the chloroplast and cytosol is linked to Fe homeostasis in plants.
2019-12-22 | GSE127300 | GEO
Project description:The biogenesis of iron-sulfur proteins in eukaryotes is an essential process involving the mitochondrial iron-sulfur cluster (ISC) assembly and export machineries and the cytosolic Fe/S protein assembly (CIA) apparatus. To define the integration of Fe/S protein biogenesis into cellular homeostasis, we compared the global transcriptional responses to defects in the three biogenesis systems in S. cerevisiae using DNA microarrays. Microarray analyses were carried out with regulatable yeast mutants in which representatives of each of the three biosynthetic systems could be depleted. In particular, we used the mutants Gal-YAH1, Gal-ATM1 and Gal-NBP35.
2007-12-14 | E-MEXP-1215 | biostudies-arrayexpress
Project description:Cytosolic iron-sulfur (Fe-S) cluster assembly (CIA) pathway delivers Fe-S clusters to nuclear and cytosolic Fe-S proteins involved in essential cellular functions. This delivery process is regulated by availability of iron and oxygen, but it remains unclear how CIA components orchestrate the cluster transfer under varying cellular environments. Here, we investigated the organization of CIA machinery under various conditions. We developed a targeted proteomics assay monitoring known CIA factors. Using this assay, we were able to detect NUBP1, CIAO3 and CIA substrates in immunoprecipitates of NUBP2, a component of the CIA scaffold complex. We also revealed that NUBP2 transiently associates with the CIA targeting complex (MMS19, CIAO1, CIAO2B), indicating the possible existence of CIA metabolons. We observed stronger interactions between CIAO3 and the CIA scaffold complex upon iron supplementation or low oxygen tension, while iron chelation and reactive oxygen species weaken CIAO3 interactions with CIA components. We further demonstrated that CIAO3 mutant with defective Fe-S cluster binding failed to integrate into the metabolons. However, these mutants unexpectedly exhibit stronger association with CIA substrates regardless of their reduced association with the CIA targeting complex, implicating that CIAO3 and CIA substrates may present in complexes independent of the CIA targeting complex. Together, our data suggested that CIA components potentially form metabolons whose assembly are regulated by environmental cues and require Fe-S cluster incorporation in CIAO3. These findings provided additional evidence that the CIA pathway adapts to changes in cellular environment through complex reorganization.
2021-11-16 | MSV000088394 | MassIVE
Project description:We performed small RNA-seq (sRNA-seq) study of Arabidopsis shoots under iron-sufficient (+Fe), iron deficient (-Fe) and iron resupply (Fe resupply) conditions to investigate and identify sRNAs whose expression is regulated by iron deficiency.
2022-09-15 | GSE209594 | GEO
Project description:Import of ferrous iron (Fe2+) via the plasma membrane ZIP transporter IRON-REGULATED TRANSPORTER1 (IRT1) bears the risk of oxidative damage and lipid peroxidation. The plasma membrane-associated SEC14-like lipid transfer protein PATL2 interacts with the large cytosolic loop and variable region of IRT1 (IRT1vr). PATL2 affects Fe reduction and reactive oxygen species-related responses in roots and alleviates lipid peroxidation upon Fe acquisition. PATL2 binds α-tocopherol, an antioxidant of the vitamin E group.
2023-04-25 | PXD032079 | Pride
Project description:Functional characterization of Arabidopsis mutants deficient in cytosolic APX1 and peroxisomal CAT2
| PRJNA122135 | ENA
Project description:Iron - sul fur (Fe -S) clusters are essential cofactors that enable proteins to transport electrons , sense signals or catalyze chemical reactions . The maturation of dozens of Fe - S proteins in various compartments of every eukaryotic cell is driven by several assembly pathways. The ubiquitous cytosolic Fe - S cluster assembly (CIA) pathway, typically composed of eight highly conserved proteins, depends on mitochondrial Fe -S cluster assembly (ISC) machinery . Giardia intestinalis contains one of the smallest eukaryotic genomes and the mitosome, an extremely reduced mitochondrion . Because the only pathway known to be retained within this organelle is the synthesis of Fe -S clusters mediated by ISC machinery, a likely function of the mitosome is to cooperate with the CIA pathway. We investigated the cellular localization of CIA components in G. intestinalis and the origin and distribution of CIA -related components and Tah18 -like proteins in other Metamonada. We show that ortholog s of Tah18 and Dre2 are missing in these eukaryotes. In Giardia, all CIA components are exclusively cytosolic , with the important exception of Cia2 and two Nbp35 paralogs, which are also present in the mitosomes. We propose that the dual localization of Cia2 and Nbp35 proteins in Giardia might represent a novel connection between the ISC and the CIA Pathways.
2016-09-29 | PXD004722 | Pride