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NFU3 is an Fe-S cluster carrier protein that is implicated in photosystem I maturation (PsaA, PsaB, PsaC). Label free proteomic approach on nfu3-2 mutant allow the discovery of new potential client proteins

ABSTRACT: NFU3 is a Fe-S cluster carrier protein of Arabidopsis that allow the maturation of Fe-S cluster proteins in chloroplast. proteomic Label free experiment was carried out to monitored wich Fe-S cluster proteins are affected in nfu3-2 mutant background

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Cotyledon, Root

SUBMITTER: Nathalie Berger

LAB HEAD: Christian Dubos

PROVIDER: PXD020228 | Pride | 2021-09-09

REPOSITORIES: Pride

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			Action	DRS
	PF_170103_NFU-col1-1.raw	Raw
	PF_170103_NFU-col1-2.raw	Raw
	PF_170103_NFU-col1-3.raw	Raw
	PF_170103_NFU-col1-4.raw	Raw
	PF_170103_NFU-col2-1.raw	Raw

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Publications

A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3.

Berger Nathalie N Vignols Florence F Touraine Brigitte B Taupin-Broggini Maël M Rofidal Valérie V Demolombe Vincent V Santoni Véronique V Rouhier Nicolas N Gaymard Frédéric F Dubos Christian C

International journal of molecular sciences 20201030 21

Iron-sulfur (Fe-S) proteins play critical functions in plants. Most Fe-S proteins are synthetized in the cytosol as apo-proteins and the subsequent Fe-S cluster incorporation relies on specific protein assembly machineries. They are notably formed by a scaffold complex, which serves for the de novo Fe-S cluster synthesis, and by transfer proteins that insure cluster delivery to apo-targets. However, scarce information is available about the maturation pathways of most plastidial Fe-S proteins an ...[more]

PMID: 33143294

Similar Datasets

E. coli monothiol glutaredoxin GrxD replenishes Fe-S clusters to the essential ErpA A-type carrier under low iron stress  

Project description:Iron-sulfur (Fe-S) clusters are required for essential biological pathways, including respiration and isoprenoid biosynthesis. Complex Fe-S cluster biogenesis systems have evolved to maintain an adequate supply of this critical protein cofactor. In Escherichia coli, two Fe-S biosynthetic systems, the “housekeeping” Isc and “stress responsive” Suf pathways, interface with a network of cluster trafficking proteins, such as ErpA, IscA, SufA, and NfuA. GrxD, a Fe-S cluster-binding monothiol glutaredoxin, also participates in Fe-S protein biogenesis in both prokaryotes and eukaryotes. Previous studies in E. coli showed that the ∆grxD mutation causes sensitivity to iron depletion, spotlighting a critical role for GrxD under conditions that disrupt Fe-S homeostasis. Here, we utilized a global chemoproteomic mass spectrometry (MS) approach to analyse the contribution of GrxD to the Fe-S proteome. Our results demonstrate that 1) GrxD is required for biogenesis of a specific subset of Fe-S proteins under iron-depleted conditions, 2) GrxD is required for cluster delivery to ErpA under iron limitation, 3) GrxD is functionally distinct from other Fe-S trafficking proteins and, 4) GrxD Fe-S cluster binding is responsive to iron limitation. All these results lead to the proposal that GrxD is required to maintain Fe-S cluster delivery to the essential trafficking protein ErpA during iron limitation conditions.

2024-07-13 | PXD053317 | Pride

METTL17 is an Fe-S cluster checkpoint for mitochondrial translation

Project description:Friedreich’s ataxia (FA) is the most common monogenic mitochondrial disease. FA is caused by a depletion of the mitochondrial protein frataxin (FXN), an iron-sulfur (Fe-S) cluster biogenesis factor. To better understand the cellular consequences of FA, we performed quantitative proteome profiling of human cells depleted for FXN. Nearly every known Fe-S cluster-containing protein was depleted in the absence of FXN, indicating that as a rule, cluster binding confers stability to Fe-S proteins. Proteomic and genetic interaction mapping identified impaired mitochondrial translation downstream of FXN loss, and specifically highlighted the methyltransferase-like protein METTL17 as a candidate effector. Using comparative sequence analysis, mutagenesis, biochemistry and cryogenic electron microscopy we show that METTL17 binds to the mitoribosomal small subunit during late assembly and harbors a previously unrecognized [Fe4S4]2+ cluster required for its stability on the mitoribosome. Notably, METTL17 overexpression rescued the mitochondrial translation and bioenergetic defects, but not the cellular growth, of FXN depleted cells. Our data suggest that METTL17 serves as an Fe-S cluster checkpoint: promoting the translation and assembly of Fe-S cluster rich OXPHOS proteins only when Fe-S cluster levels are replete.

2023-12-27 | PXD045443 | Pride

Cytosolic Fe-S cluster assembly-deficient mutant, nar1 and nbp35 mutant seedling

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

Monitoring Fe-S cluster occupancy across the E. coli proteome using chemoproteomics

Project description:Iron-sulfur (Fe-S) clusters are ubiquitous metallocofactors involved in redox chemistry, radical generation, and gene regulation. Common methods to monitor Fe-S clusters include spectroscopic analysis of purified proteins, and auto-radiographic visualization of radiolabeled iron distribution in proteomes. Here, we report a chemoproteomic strategy that monitors changes in the reactivity of Fe-S cysteine ligands to inform on Fe-S cluster occupancy. We highlight the utility of this platform in E. coli by: (1) demonstrating global disruptions in Fe-S incorporation in cells cultured under iron-depleted conditions; (2) determining Fe-S client proteins reliant on three scaffold/carrier proteins within the Isc Fe-S biogenesis pathway; and, (3) identifying two previously unannotated Fe-S proteins, TrhP and DppD. In summary, the chemoproteomic strategy described herein is a powerful tool that reports on Fe-S cluster incorporation directly within a native proteome, and enables the interrogation of Fe-S biogenesis pathways, and the identification of previously uncharacterized Fe-S proteins.

2024-05-22 | PXD026488 | Pride

The plastidial Arabidopsis thaliana NFU1 delivers [4Fe-4S] clusters to specific client proteins

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

Physiological and transcriptomic characterization of white lupin response to Fe deficiency

Project description:Iron (Fe) and phosphorus (P) are essential nutrients for plants growth. Despite their abundance in soils, they are barely available for plants. In order to overcome these nutritional stresses, plants have evolved strategies including physiological, biochemical and morphological adaptations. Biosynthesis and release of low molecular weight compounds from the roots play a crucial role in P and Fe mobilization. White lupin (Lupinus albus L.) is considered a model plant for studying root exudates and for P-deficient adaptation. White lupin is able to markedly modify its root architecture by forming special structures called cluster roots, and modifies the rhizospheric soil characteristics by biosynthesising and releasing great amounts of exudates. These phenomena are quite well described in response to P deficiency, but there is few information on the adaptation of a cluster-root producing plant species to Fe deficiency. This prompted this work, aimed to characterize the physiological and transcriptomic responses of white lupin plants to Fe deficiency. Occurrence of Strategy I components and interactions with P nutrition has been also investigated in this work. Results showed a physiological and transcriptional link between the responses to Fe and P deficiency in white lupin roots. Phosphorus-deficient plants activated the Strategy I Fe acquisition mechanisms that lead to an enhanced Fe mobilization and translocation and that might help the P acquisition process. On the other hand, also the Fe deficiency enhanced the phosphate acquisition and some P-deficient-responsive genes were overexpressed.

2019-03-22 | GSE112220 | GEO

RNA-seq analysis of Arabidopsis roots of Col-0, fls2 and UBQ10::mCitrine-IMA1 in response to +Fe, +Fe+flg22, -Fe and -Fe+flg22

Project description:We reported the flg22-triggered immune responses in roots affect the iron deficiency responses and may link to the function of FLS2 and IMA1 in the root. To identify the underlying mechanism of how the root transcriptome profiles respond to +Fe, +Fe+flg22, -Fe, -Fe+flg22 respectively, and if the flg22 responses is dependent on the function of FLS2 and IMA1 in the root, we performed an mRNA-seq experiments in Col-0, fls2 and UBQ10::mCitrine-IMA1 with different treatments. The differentially expressed genes in response to +Fe, +Fe+flg22, -Fe, -Fe+flg22 were analyzed. It has 36 samples in total, with 3 biogical replicates for each condition and each genotype.

2023-10-09 | GSE213557 | GEO

Fe-FIT-Diff

Project description:au13-06_fit - Fe-FIT-Diff - FIT (FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR) is a regulator of Fe deficiency responses in the root. FIT is a basic helix-loop-helix protein. Here, we investigated the transcriptome changes in response to Fe deficiency (- Fe) versus the control condition (+ Fe) in wild type, the fit-3 loss of function mutant and in FIT overexpression plants.

2015-02-14 | GSE65934 | GEO

Cytosolic Fe-S cluster assembly-deficient mutant, nar1 and nbp35 mutant seedling

2013-05-01 | E-GEOD-44116 | biostudies-arrayexpress

response of ein3eil1 mutants to fe deficiency-Role of ethylene in Fe deficieny response signalling

Project description:au10-14_fer - response of ein3eil1 mutants to fe deficiency - Response of ein3eil1 mutants to Fe deficiency - Wild type seedlings and ethylene insensitive ein3eil1 seedlings were germinated and grown in the presence of 50 µM Fe or absence of Fe (0 µM) on Hoagland medium agar plates until the age of 6 days. Under these growth conditions symptoms of Fe deficiency develop in the 0 Fe plants. Ethylene is known to promote Fe acquisition responses. Whole seedlings were harvested for transcriptome analysis, in a total of three biological replicates.

2011-12-31 | GSE26510 | GEO

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