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    iscU scaffold protein for iron-sulfur cluster assembly [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947002, updated on 3-Dec-2024

    Summary

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    Official Symbol
    iscU
    Official Full Name
    scaffold protein for iron-sulfur cluster assembly
    Primary source
    ECOCYC:G7324
    Locus tag
    b2529
    See related
    ASAP:ABE-0008321
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK2526; nifU; yfhN
    Summary
    IscU fails to assemble Fe-S clusters in the presence of sodium citrate due to restricted free iron availability, however Fe-S cluster formation is restored, with sodium citrate present, in the presence of IscA. [More information is available at EcoGene: EG13395]. The iscSUA operon plays a role in assembly (or maintenance) of iron-sulfur clusters . [More information is available at EcoCyc: G7324].
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    Genomic context

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    Sequence:
    NC_000913.3 (2659903..2660289, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene [Fe-S] cluster biosynthesis co-chaperone HscB Neighboring gene iron-sulfur cluster insertion protein IscA Neighboring gene cysteine desulfurase IscS Neighboring gene DNA-binding transcriptional dual regulator IscR

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Frazzon J, et al. Biochem Soc Trans, 2002 Aug. PMID 12196163
    2. Fe-S cluster assembly pathways in bacteria. Ayala-Castro C, et al. Microbiol Mol Biol Rev, 2008 Mar. PMID 18322036, Free PMC Article
    3. Iron-sulfur cluster biosynthesis. Bandyopadhyay S, et al. Biochem Soc Trans, 2008 Dec. PMID 19021507, Free PMC Article
    4. Bacterial IscU is a well folded and functional single domain protein. Adinolfi S, et al. Eur J Biochem, 2004 Jun. PMID 15153099
    5. The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein. Iannuzzi C, et al. PLoS One, 2011. PMID 21799759, Free PMC Article

    See all (69) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Iron-sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichiacoli.
      Title: Iron-sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichiacoli.
    2. Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.
      Title: Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.
    3. We have demonstrated that a single mutation in the scaffold protein IscU rendered E. coli viability strictly dependent upon a functional CyaY.
      Title: Turning Escherichia coli into a Frataxin-Dependent Organism.
    4. Data indicate that the single point mutation IscU_D39A affects the 2Fe-2S coordination geometry.
      Title: Anatomy of an iron-sulfur cluster scaffold protein: Understanding the determinants of [2Fe-2S] cluster stability on IscU.
    5. Data indicate that IscU exists as two interconverting species: one (S) is largely structured with all four peptidyl-prolyl bonds trans; the other (D) contains an ordered domain that stabilizes two cis peptidyl-prolyl peptide bonds.
      Title: Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery.
    6. The iron-sulfur cluster assembly in E. coli IscU is an IscS mediated biosynthetic process.
      Title: Biochemical characterization of iron-sulfur cluster assembly in the scaffold IscU of Escherichia coli.
    7. study determined the crystal structures of IscS-IscU and IscS-TusA complexes providing the first insight into their different modes of binding and the mechanism of sulfur transfer
      Title: Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions.
    8. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU
      Title: Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU.
    9. Escherichia coli CYaY is an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
      Title: Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU.
    10. both iron-sulfur cluster assembly protein IscU and co-chaperone HscB interact with the low peptide affinity T-state conformation of HscA ATPase and both modestly accelerate the rate-determining steps in the HscA reaction cycle
      Title: Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 2 iron, 2 sulfur cluster binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 2 iron, 2 sulfur cluster binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 4 iron, 4 sulfur cluster binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables copper ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ferrous iron binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables iron ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables iron-sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in L-cysteine catabolic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in intracellular iron ion homeostasis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in iron-sulfur cluster assembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in iron-sulfur cluster assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in iron-sulfur cluster assembly NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of IscS-IscU complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    scaffold protein for iron-sulfur cluster assembly

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      2659903..2660289 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417024.1 scaffold protein for iron-sulfur cluster assembly [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417024.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A1V2GF16, A0A5B9AR62
      Conserved Domains (1) summary
      PRK11325
      Location:1 → 127
      PRK11325; scaffold protein; Provisional
    Nucleotide Protein
    Heading Accession and Version

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