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Search results 1 to 100 out of 136 for Iscu

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Hits by Strain

Type Details Score
Gene
23479 | ISCU
Type: gene
Organism: human
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Gene
394688 | iscu
Type: gene
Organism: frog, western clawed
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Gene
288740 | Iscu
Type: gene
Organism: rat
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Gene
477527 | ISCU
Type: gene
Organism: dog, domestic
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Gene
452209 | ISCU
Type: gene
Organism: chimpanzee
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Gene
514789 | ISCU
Type: gene
Organism: cattle
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Gene
416891 | ISCU
Type: gene
Organism: chicken
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Gene
705669 | ISCU
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:1913633 | Iscu
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
- | J:324324
     
First Author: Birling M-C
Year: 2021
Journal: Direct Data Submission
Title: Direct Data Submission for Alpk1 and Iscu alleles.
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Publication
21165651 | J:339029
First Author: Nordin A
Year: 2011
Journal: Hum Genet
Title: Tissue-specific splicing of ISCU results in a skeletal muscle phenotype in myopathy with lactic acidosis, while complete loss of ISCU results in early embryonic death in mice.
Volume: 129
Issue: 4
Pages: 371-8
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Publication
23508953 | J:198599
First Author: La P
Year: 2013
Journal: J Biol Chem
Title: Mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation stabilizes ISCU protein: implications for iron metabolism.
Volume: 288
Issue: 18
Pages: 12901-9
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Publication
25597503 | J:326895
 
First Author: Parent A
Year: 2015
Journal: Nat Commun
Title: Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols.
Volume: 6
Pages: 5686
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Publication
17603005 | J:126883
First Author: Canal F
Year: 2007
Journal: Arch Biochem Biophys
Title: Regulation of the cysteine desulfurase Nfs1 and the scaffold protein IscU in macrophages stimulated with interferon-gamma and lipopolysaccharide.
Volume: 465
Issue: 1
Pages: 282-92
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Publication
29097656 | J:320071
First Author: Boniecki MT
Year: 2017
Journal: Nat Commun
Title: Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.
Volume: 8
Issue: 1
Pages: 1287
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Protein Coding Gene
MGP_CAROLIEiJ_G0027581 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0029923 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0029888 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0029826 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0029899 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0029619 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1913633 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0030353 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0029027 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0029586 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0029736 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0029693 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0029825 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0029724 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0030394 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0028741 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0029103 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0024163 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0028579 | -
Type: protein_coding_gene
Organism: Mus spretus
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GXD Expression
GXD Expression
 
Probe: MGI:7624147
Assay Type: Immunohistochemistry
Annotation Date: 2024-04-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3187817
Pattern: Not Specified
Stage: TS17
Assay Id: MGI:7624266
Age: embryonic day 10.5
Image: 6I Ctcf fl/+; Tie2-Cre; Rosa mT/mG/+
Specimen Label: 6I Ctcf fl/+; Tie2-Cre; Rosa mT/mG/+
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
Probe: MGI:7624147
Assay Type: Immunohistochemistry
Annotation Date: 2024-04-26
Strength: Weak
Sex: Not Specified
Emaps: EMAPS:3187817
Pattern: Not Specified
Stage: TS17
Assay Id: MGI:7624266
Age: embryonic day 10.5
Image: 6I Ctcf fl/fl; Tie2-Cre; Rosa mT/mG/+
Note: Decreased expression in endothelial cell nuclei compared to control.
Specimen Label: 6I Ctcf fl/fl; Tie2-Cre; Rosa mT/mG/+
Detected: true
Specimen Num: 2
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Publication
27519411 | J:320072
First Author: Gakh O
Year: 2016
Journal: J Biol Chem
Title: Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery.
Volume: 291
Issue: 40
Pages: 21296-21321
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Publication
17597094 | J:129870
First Author: Martelli A
Year: 2007
Journal: Hum Mol Genet
Title: Frataxin is essential for extramitochondrial Fe-S cluster proteins in mammalian tissues.
Volume: 16
Issue: 22
Pages: 2651-8
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Publication
19808020 | J:153662
First Author: Chan SY
Year: 2009
Journal: Cell Metab
Title: MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2.
Volume: 10
Issue: 4
Pages: 273-84
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Publication
16286020 | J:113295
First Author: Rubtsov A
Year: 2005
Journal: Immunity
Title: Lsc regulates marginal-zone B cell migration and adhesion and is required for the IgM T-dependent antibody response.
Volume: 23
Issue: 5
Pages: 527-38
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Publication
21298097 | J:327042
First Author: Schmucker S
Year: 2011
Journal: PLoS One
Title: Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.
Volume: 6
Issue: 1
Pages: e16199
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Publication
29610276 | J:264015
First Author: Roy AR
Year: 2018
Journal: J Biol Chem
Title: The transcriptional regulator CCCTC-binding factor limits oxidative stress in endothelial cells.
Volume: 293
Issue: 22
Pages: 8449-8461
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Publication
14651853 | J:86816
First Author: Mootha VK
Year: 2003
Journal: Cell
Title: Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.
Volume: 115
Issue: 5
Pages: 629-40
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Publication
18614015 | J:151002
First Author: Pagliarini DJ
Year: 2008
Journal: Cell
Title: A mitochondrial protein compendium elucidates complex I disease biology.
Volume: 134
Issue: 1
Pages: 112-23
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Publication
- | J:77000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: MGC Data curation in Mouse Genome Informatics
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Publication
- | J:81858
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Gene
738449 | LOC738449
Type: gene
Organism: chimpanzee
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
16964969 | -
First Author: Chandramouli K
Year: 2006
Journal: Biochemistry
Title: HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.
Volume: 45
Issue: 37
Pages: 11087-95
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Protein Domain
IPR011339 | ISC_FeS_clus_asmbl_IscU
Type: Family
Description: Iron-sulphur(FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents IscU from the ISC system, a homologue of the N-terminal region of NifU (NIF system), an Fe-S cluster assembly protein found mostly in nitrogen-fixing bacteria. IscU is a scaffold protein on which Fe-S clusters are assembled before transfer to apoproteins []. This family includes largely proteobacterial and eukaryotic forms and excludes the true NifU proteins from Klebsiella sp. and Anabaena sp. as well as the archaeal homologues.
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UniProt Feature
UniProt Feature
Begin: 383
Description: Iron-sulfur (2Fe-2S); via persulfide group; shared with ISCU
Type: metal ion-binding site
End: 383
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GO Term
GO:0099128 | mitochondrial [2Fe-2S] assembly complex
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Protein
Q9D7P6
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
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Protein
D3Z0K9
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: true
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Publication
11053447 | -
First Author: Silberg JJ
Year: 2001
Journal: J Biol Chem
Title: The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli.
Volume: 276
Issue: 3
Pages: 1696-700
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GO Term
GO:1990330 | IscS-IscU complex
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Publication
16211402 | -
First Author: Fontecave M
Year: 2005
Journal: J Biol Inorg Chem
Title: Mechanisms of iron-sulfur cluster assembly: the SUF machinery.
Volume: 10
Issue: 7
Pages: 713-21
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Publication
16843540 | -
First Author: Lill R
Year: 2006
Journal: Biochim Biophys Acta
Title: Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes.
Volume: 1763
Issue: 7
Pages: 652-67
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Publication
15937904 | -
First Author: Shimomura Y
Year: 2005
Journal: Proteins
Title: Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters.
Volume: 60
Issue: 3
Pages: 566-9
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Publication
16221578 | -
 
First Author: Barras F
Year: 2005
Journal: Adv Microb Physiol
Title: How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.
Volume: 50
Pages: 41-101
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Publication
8875867 | -
First Author: Hwang DM
Year: 1996
Journal: J Mol Evol
Title: A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.
Volume: 43
Issue: 5
Pages: 536-40
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Publication
17350000 | -
First Author: Sendra M
Year: 2007
Journal: FEBS Lett
Title: The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA.
Volume: 581
Issue: 7
Pages: 1362-8
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Publication
15278785 | -
First Author: Ollagnier-de-Choudens S
Year: 2004
Journal: J Biol Inorg Chem
Title: SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly.
Volume: 9
Issue: 7
Pages: 828-38
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Publication
11498000 | -
First Author: Seidler A
Year: 2001
Journal: Biochem Soc Trans
Title: Incorporation of iron-sulphur clusters in membrane-bound proteins.
Volume: 29
Issue: Pt 4
Pages: 418-21
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Publication
34669463 | J:314362
First Author: Negi V
Year: 2021
Journal: Sci Adv
Title: Computational repurposing of therapeutic small molecules from cancer to pulmonary hypertension.
Volume: 7
Issue: 43
Pages: eabh3794
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Publication
25825391 | J:229258
First Author: White K
Year: 2015
Journal: EMBO Mol Med
Title: Genetic and hypoxic alterations of the microRNA-210-ISCU1/2 axis promote iron-sulfur deficiency and pulmonary hypertension.
Volume: 7
Issue: 6
Pages: 695-713
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Publication
19965627 | J:156835
First Author: Crooks DR
Year: 2010
Journal: Blood
Title: Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery.
Volume: 115
Issue: 4
Pages: 860-9
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Publication
24983771 | J:218499
First Author: Hale A
Year: 2014
Journal: Biochim Biophys Acta
Title: An Argonaute 2 switch regulates circulating miR-210 to coordinate hypoxic adaptation across cells.
Volume: 1843
Issue: 11
Pages: 2528-42
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Publication
32073141 | J:291823
First Author: Nakada C
Year: 2020
Journal: J Pathol
Title: A transgenic mouse expressing miR-210 in proximal tubule cells shows mitochondrial alteration: possible association of miR-210 with a shift in energy metabolism.
Volume: 251
Issue: 1
Pages: 12-25
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Protein Domain
IPR036762 | IscX-like_sf
Type: Homologous_superfamily
Description: The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].This entry represents IscX proteins (also known as hypothetical protein YfhJ) that are part of the ISC system. IscX is active as a monomer. The structure of YfhJ is an orthogonal α-bundle []. YfhJ is a small acidic protein that binds IscS, and contains a modified winged helix motif that is usually found in DNA-binding proteins []. YfhJ/IscX can bind Fe, and may function as an Fe donor in the assembly of FeS clusters
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Publication
16698547 | -
First Author: Pastore C
Year: 2006
Journal: Structure
Title: YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein?
Volume: 14
Issue: 5
Pages: 857-67
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Publication
15100228 | -
First Author: Tapley TL
Year: 2004
Journal: J Biol Chem
Title: Preferential substrate binding orientation by the molecular chaperone HscA.
Volume: 279
Issue: 27
Pages: 28435-42
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Protein Domain
IPR010236 | ISC_FeS_clus_asmbl_HscA
Type: Family
Description: Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the HscA chaperone protein from the SUF system. HscA (or Hsc66) is a specialised bacterial Hsp70-class molecular chaperone that participates in the assembly of iron-sulphur cluster proteins. HscA resembles DnaK, but belongs to a separate clade. HscA interacts with IscU, which is believed to serve as a template for Fe-S cluster formation. The HscA-IscU interaction is facilitated by the J-type co-chaperone protein HscB (or Hsc20), which binds to both HscA and IscU, bringing them into contact with each other. HscA recognises a conserved LPPVK sequence motif at positions 99-103 of IscU [].
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Protein Domain
IPR007479 | ISC_FeS_clus_asmbl_IscsX
Type: Family
Description: Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].This entry represents IscX proteins (also known as hypothetical protein YfhJ) that are part of the ISC system. IscX is active as a monomer. The structure of YfhJ is an orthogonal α-bundle []. YfhJ is a small acidic protein that binds IscS, and contains a modified winged helix motif that is usually found in DNA-binding proteins []. YfhJ/IscX can bind Fe, and may function as an Fe donor in the assembly of FeS clusters
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Protein Domain
IPR034904 | FSCA_dom_sf
Type: Homologous_superfamily
Description: Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and oneprotein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].
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