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

ABSTRACT: 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).

ORGANISM(S): Arabidopsis thaliana

SUBMITTER: Miyuki Nakamura

PROVIDER: E-GEOD-44116 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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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

Transcription profiling of yeast mutants Gal-YAH1, Gal-ATM1 and Gal-NBP35 to investigate responses to defects in cellular Fe-S protein maturation

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2007-12-14 | E-MEXP-1215 | biostudies-arrayexpress

Incomplete cytosolic iron-sulfur cluster assembly machinery of Giardia intestinalis is partially associated with mitosomes

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

Iron-Regulated Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery

Project description:The 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. Although the delivery process is regulated by the availability of iron and oxygen, it remains unclear how CIA components orchestrate the cluster transfer under varying cellular environments. Here, we utilized a targeted proteomics assay for monitoring CIA factors and substrates to characterize the CIA machinery. We find that NUBP1 (NBP35), CIAO3 (NARFL) and CIA substrates associate with NUBP2 (CFD1), a component of the CIA scaffold complex. We also show that NUBP2 weakly associates with the CIA targeting complex (MMS19, CIAO1, CIAO2B) indicating the possible existence of a higher order complex. Interactions between CIAO3 and the CIA scaffold complex are strengthened upon iron supplementation or low oxygen tension, while iron chelation and reactive oxygen species weaken CIAO3 interactions with CIA components. We further demonstrate that CIAO3 mutants defective in Fe-S cluster binding fail to integrate into the higher order complexes. However, these mutants exhibit stronger associations with CIA substrates under conditions in which the association with the CIA targeting complex is reduced suggesting that CIAO3 and CIA substrates may associate in complexes independently of the CIA targeting complex. Together, our data suggest that CIA components potentially form a metabolon whose assembly is regulated by environmental cues and requires Fe-S cluster incorporation in CIAO3. These findings provide additional evidence that the CIA pathway adapts to changes in cellular environment through complex reorganization.

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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

Dynamic Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery Requires Iron-Sulfur Cluster Incorporation of CIAO3

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.

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Fe-S clusters-binding proteins in mitoribosome

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2024-01-26 | PXD039321 | Pride

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

Project description: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

2021-09-09 | PXD020228 | Pride

Expression analysis of N. europaea (ATCC 19718) wildtype and pFur::Kan mutant grown in Fe-replete and Fe-limited media

Project description:Investigation of whole genome gene expression level changes in a Nitrosomonas europaea (ATCC 19718) wildtype and pFur::Kan mutant [kanamycin resistance cassette insertion in the promoter region of the fur gene (NE0616)] strains grown in Fe-replete and Fe-limited media. The Nitrosomonas europaea (ATCC 19718) wiltype cells grown in Fe-limited media were compared to cells grown in Fe-replete media to gain a better understanding of the metabolic changes occurring in response to iron stress. The Nitrosomonas europaea (ATCC 19718) pFur::Kan mutant strain grown in Fe-replete & Fe-limited media were compared to wildtype cells grown in Fe=replete & Fe-limited media to gain a better understanding of the role Fur (NE0616) plays in iron homeostasis control.

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