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ProteomicsIron-Regulated Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery
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...
ORGANISM(S): Homo Sapiens 
2022-06-06 | PXD033557 | panorama
ProteomicsFeS protein levels in Arabidopsis plants expressing a mutated NEET protein
Iron-sulfur (Fe-S) clusters play an essential role in plants as protein co-factors mediating diverse electron transfer reactions. Because they can react with oxygen to form reactive oxygen species (ROS) and cause cellular damage, the biogenesis of Fe-S clusters is highly regulated. A newly discovere...
ORGANISM(S): Arabidopsis Thaliana 
2021-01-24 | PXD015447 | panorama
TranscriptomicsM. sedula transcriptional response to ferrous iron and RISC supplements
Abstract: The crenarchaeal order Sulfolobales collectively contains at least five major terminal oxidase complexes. Based on genome sequence information, all five complexes are found only in Metallosphaera sedula and Sulfolobus tokodaii, the two sequenced Sulfolobales capable of iron oxidization. Wh...
ORGANISM(S): Metallosphaera sedula 
2008-10-22 | E-GEOD-12044 | biostudies-arrayexpress
ProteomicsDynamic Assembly of the Cytosolic Iron-Sulfur Cluster Biogenesis Machinery Requires Iron-Sulfur Cluster Incorporation of CIAO3
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...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-11-16 | MSV000088394 | MassIVE
TranscriptomicsIscR of Rhodobacter sphaeroides functions as repressor of genes for iron-sulphur metabolism and represents a new type of iron-sulphur binding protein
Iron-sulphur (Fe-S) clusters are ensembles of iron and sulphide centres. They are found in all life forms and are important components of many enzymes involved in diverse cellular processes, including respiration, DNA synthesis or gene regulation. However, the increase in oxygen after the emergence...
ORGANISM(S): Rhodobacter sphaeroides 2.4.1 
2015-02-03 | E-GEOD-65537 | biostudies-arrayexpress
TranscriptomicsIscR of Rhodobacter sphaeroides functions as repressor of genes for iron-sulphur metabolism and represents a new type of iron-sulphur binding protein
Iron-sulphur (Fe-S) clusters are ensembles of iron and sulphide centres. They are found in all life forms and are important components of many enzymes involved in diverse cellular processes, including respiration, DNA synthesis or gene regulation. However, the increase in oxygen after the emergence ...
ORGANISM(S): Cereibacter sphaeroides 2.4.1 
2015-02-03 | GSE65537 | GEO
ProteomicsDrosophila NFS1.R77 is required for differential protein complex composition
S-adenosylmethionine (SAM) is the principle biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane SAMC and supports the m...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-02-22 | PXD019551 | Pride
Nfs1 Drosophila Iron sulphur clusters 
UnknownIron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis.
Not available
S-EPMC3569480 | biostudies-literature
UnknownCopper binding in IscA inhibits iron-sulphur cluster assembly in Escherichia coli.
Not available
S-EPMC4132641 | biostudies-literature
TranscriptomicsChemical potentiator of copper-accumulation and -toxicity: Probing iron- regulons of Saccharomyces cerevisiae
RNA-seq was used to assess mRNA transcript abundance in wild type and fra2M-NM-^T S. cerevisiae (BY4741) cells treated with 2-(6-benzyl-2-pyridyl)quinazoline (BPQ) and CuSO4. BPQ potentiates copper toxicity and in yeast, in common with other organisms, a major cause of copper toxicity is damage of i...
ORGANISM(S): Saccharomyces cerevisiae 
2014-06-04 | E-GEOD-54045 | biostudies-arrayexpress
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