A metazoan ATAC acetyltransferase subunit that regulates mitogen-activated protein kinase signaling is related to an ancient molybdopterin synthase component.

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  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 101125647 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1535-9484 (Electronic) Linking ISSN: 15359476 NLM ISO Abbreviation: Mol Cell Proteomics Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Bethesda, MD : American Society for Biochemistry and Molecular Biology, [2002-
    • Subject Terms:
      MAP Kinase Signaling System*; Drosophila melanogaster/*enzymology ; Protein Subunits/*physiology ; Sulfurtransferases/*genetics ; Sulfurtransferases/*physiology; Algorithms ; Animals ; Cell Line ; Conserved Sequence ; Enzyme Activation ; Evolution, Molecular ; Immunoprecipitation ; Molecular Sequence Data ; Phylogeny ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Quaternary ; Protein Subunits/isolation & purification ; Protein Subunits/metabolism ; Sequence Analysis, Protein ; Sulfurtransferases/isolation & purification ; Sulfurtransferases/metabolism
    • Abstract:
      Molybdopterin (MPT) synthase is an essential enzyme involved in the synthesis of the molybdenum cofactor precursor molybdopterin. The molybdenum cofactor biosynthetic pathway is conserved from prokaryotes to Metazoa. CG10238 is the Drosophila homolog of the MoaE protein, a subunit of MPT synthase, and is found in a fusion with the mitogen-activated protein kinase (MAPK)-upstream protein kinase-binding inhibitory protein (MBIP). This fused protein inhibits the activation of c-Jun N-terminal kinase (JNK). dMoaE (CG10238) carries out this function as a subunit of the ATAC histone acetyltransferase complex. In this study, we demonstrate that Drosophila MoaE (CG10238) also interacts with Drosophila MoaD and with itself to form a complex with stoichiometry identical to the MPT synthase holoenzyme in addition to its function in ATAC. We also show that sequence determinants that regulate MAPK signaling are located within the MoaE region of dMoaE (CG10238). Analysis of other metazoan MBIPs reveals that MBIP protein sequences have an N-terminal region that appears to have been derived from the MoaE protein, although it has lost residues responsible for catalytic activity. Thus, intact and modified copies of the MoaE protein may have been conscripted to play a new, noncatalytic role in MAPK signaling in Metazoa as part of the ATAC complex.
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    • Accession Number:
      0 (Protein Subunits)
      EC 2.8.1.- (Sulfurtransferases)
      EC 2.8.1.- (molybdopterin synthase)
    • Publication Date:
      Date Created: 20120221 Date Completed: 20120917 Latest Revision: 20211021
    • Publication Date:
      20240829
    • Accession Number:
      PMC3418850
    • Accession Number:
      10.1074/mcp.M111.015818
    • Accession Number:
      22345504