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Search results 1 to 100 out of 145 for Hscb

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Hits by Strain

Type Details Score
Gene
150274 | HSCB
Type: gene
Organism: human
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Gene
779876 | hscb
Type: gene
Organism: frog, western clawed
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Gene
360826 | Hscb
Type: gene
Organism: rat
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Gene
477531 | HSCB
Type: gene
Organism: dog, domestic
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Gene
458734 | HSCB
Type: gene
Organism: chimpanzee
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Gene
786040 | HSCB
Type: gene
Organism: cattle
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Gene
768938 | HSCB
Type: gene
Organism: chicken
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Gene
100150029 | hscb
Type: gene
Organism: zebrafish
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Gene
713734 | HSCB
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:2141135 | Hscb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR004640 | HscB
Type: Family
Description: The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein []. This process is facilitated by a specialized chaperone system, which consists of a molecular chaperone from the Hsc70 family, HscA in E. coli, and a co-chaperone of the J-domain family, Hsc20/HscB (known as Jac1 in fungi) []. The co-chaperone HscB recruits the scaffold protein for Fe-S cluster biogenesis Isu1/IscU, guiding it to the chaperone HscA [, ], and enhances the intrinsic ATPase activity of the HscA [].
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Publication
32634119 | J:290037
     
First Author: Crispin A
Year: 2020
Journal: J Clin Invest
Title: Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia.
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Protein
Q8K3A0
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
A0A0R4J0T0
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
F6UL52
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Publication
15485839 | -
First Author: Silberg JJ
Year: 2004
Journal: J Biol Chem
Title: Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.
Volume: 279
Issue: 52
Pages: 53924-31
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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 Coding Gene
MGP_CAROLIEiJ_G0027553 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0029894 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0029860 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0029798 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0029871 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0029591 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_2141135 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0030324 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0028999 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0029558 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0029708 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0029665 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0029796 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0029696 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0030365 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0028713 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0029075 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0024135 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0028551 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
22306468 | -
First Author: Ciesielski SJ
Year: 2012
Journal: J Mol Biol
Title: Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution.
Volume: 417
Issue: 1-2
Pages: 1-12
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Publication
12970193 | -
First Author: Mühlenhoff U
Year: 2003
Journal: EMBO J
Title: Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p.
Volume: 22
Issue: 18
Pages: 4815-25
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Publication
16551614 | -
First Author: Andrew AJ
Year: 2006
Journal: J Biol Chem
Title: Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p.
Volume: 281
Issue: 21
Pages: 14580-7
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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:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:57656
     
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
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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
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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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
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:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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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:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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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
- | 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
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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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:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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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: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: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:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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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
- | 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: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:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Gene
444532 | hscb.L
Type: gene
Organism: frog, African clawed
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Protein
F6WN43
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Allele
Hscb<+> | MGI:3690043
 
Name: HscB iron-sulfur cluster co-chaperone; wild type
Allele Type: Not Specified
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Publication
18713742 | -
First Author: Bitto E
Year: 2008
Journal: J Biol Chem
Title: Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.
Volume: 283
Issue: 44
Pages: 30184-92
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Allele
Hscb<Gt(OST16900)Lex> | MGI:4141475
 
Name: HscB iron-sulfur cluster co-chaperone; gene trap OST16900, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Hscb<Gt(OST28640)Lex> | MGI:4149356
 
Name: HscB iron-sulfur cluster co-chaperone; gene trap OST28640, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Hscb<Gt(OST31291)Lex> | MGI:4151234
 
Name: HscB iron-sulfur cluster co-chaperone; gene trap OST31291, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Hscb<Gt(OST97314)Lex> | MGI:4181933
 
Name: HscB iron-sulfur cluster co-chaperone; gene trap OST97314, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Hscb<Gt(OST269080)Lex> | MGI:4257899
 
Name: HscB iron-sulfur cluster co-chaperone; gene trap OST269080, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Hscb<tm1a(EUCOMM)Wtsi> | MGI:4432940
Name: HscB iron-sulfur cluster co-chaperone; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
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Allele
Hscb<tm1e(EUCOMM)Wtsi> | MGI:4433025
Name: HscB iron-sulfur cluster co-chaperone; targeted mutation 1e, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hscb<tm1e(EUCOMM)Hmgu> | MGI:5299776
Name: HscB iron-sulfur cluster co-chaperone; targeted mutation 1e, Helmholtz Zentrum Muenchen GmbH
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Hscb<tm1a(EUCOMM)Hmgu> | MGI:5299865
Name: HscB iron-sulfur cluster co-chaperone; targeted mutation 1a, Helmholtz Zentrum Muenchen GmbH
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
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Allele
Hscb<tm1c(EUCOMM)Hmgu> | MGI:6438165
Name: HscB iron-sulfur cluster co-chaperone; targeted mutation 1c, Helmholtz Zentrum Muenchen GmbH
Allele Type: Targeted
Attribute String: Conditional ready, No functional change
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Allele
Hscb<em1(IMPC)Kmpc> | MGI:7761794
Name: HscB iron-sulfur cluster co-chaperone; endonuclease-mediated mutation 1, Korea Mouse Phenotyping Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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DO Term
DOID:0061007 | sideroblastic anemia 5
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Strain
MGI:6438166 | B6J.B6N(129S4)-Hscb<tm1c(EUCOMM)Hmgu>/MdfMmjax
Attribute String: congenic, mutant strain, targeted mutation
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Protein Domain
IPR036386 | HscB_C_sf
Type: Homologous_superfamily
Description: This superfamily represents the C-terminal oligomerisation domain found in HscB (heat shock cognate protein B), which is also known as HSC20 (20K heat shock cognate protein) and J-protein Jac1 in yeast mitochondria []. HscB acts as a co-chaperone to regulate the ATPase activity and peptide-binding specificity of the molecular chaperone HscA, also known as HSC66 (HSP70 class). HscB proteins contain two domains, an N-terminal J-domain, which is involved in interactions with HscA, connected by a short loop to the C-terminal oligomerisation domain; the two domains make contact through a hydrophobic interface. The core of the oligomerisation domain is thought to bind and target proteins to HscA and consists of an open, three-helical bundle []. HscB, along with HscA, has been shown to play a role in the biogenesis of iron-sulphur proteins.
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Protein Domain
IPR009073 | HscB_oligo_C
Type: Domain
Description: This entry represents the C-terminal oligomerisation domain found in HscB (heat shock cognate protein B), which is also known as HSC20 (20K heat shock cognate protein) and J-protein Jac1 in yeast mitochondria []. HscB acts as a co-chaperone to regulate the ATPase activity and peptide-binding specificity of the molecular chaperone HscA, also known as HSC66 (HSP70 class). HscB proteins contain two domains, an N-terminal J-domain, which is involved in interactions with HscA, connected by a short loop to the C-terminal oligomerisation domain; the two domains make contact through a hydrophobic interface. The core of the oligomerisation domain is thought to bind and target proteins to HscA and consists of an open, three-helical bundle []. HscB, along with HscA, has been shown to play a role in the biogenesis of iron-sulphur proteins.
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Publication
11124030 | -
First Author: Cupp-Vickery JR
Year: 2000
Journal: J Mol Biol
Title: Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.
Volume: 304
Issue: 5
Pages: 835-45
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Protein Domain
IPR040682 | HscB_4_cys
Type: Domain
Description: This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed β-hairpins. Although the N-domain lacks anyrecognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin [].
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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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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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Protein
Q9D7P6
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
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