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Biological iron-sulfur storage in a thioferrate-protein nanoparticle

Author

Listed:
  • Brian J. Vaccaro

    (University of Georgia
    University of Georgia)

  • Sonya M. Clarkson

    (University of Georgia
    Present address: Conagen Inc., 15 DeAngelo Dr., Bedford, Massachusetts 01730, USA)

  • James F. Holden

    (University of Georgia
    Present address: Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003, USA)

  • Dong-Woo Lee

    (University of Georgia
    Present address: Laboratory of Applied Biochemistry, School of Applied Biosciences, Kyungpook National University, Daegu 41566, Korea)

  • Chang-Hao Wu

    (University of Georgia)

  • Farris L. Poole II

    (University of Georgia)

  • Julien J. H. Cotelesage

    (University of Saskatchewan)

  • Mark J. Hackett

    (University of Saskatchewan
    Present address: Department of Chemistry, Curtin University, Perth, Western Australia 6102, Australia)

  • Sahel Mohebbi

    (University of Georgia)

  • Jingchuan Sun

    (Cryo-EM Structural Biology Laboratory, Center for Epigenetics, Van Andel Research Institute)

  • Huilin Li

    (Cryo-EM Structural Biology Laboratory, Center for Epigenetics, Van Andel Research Institute)

  • Michael K. Johnson

    (University of Georgia)

  • Graham N. George

    (University of Saskatchewan)

  • Michael W. W. Adams

    (University of Georgia)

Abstract

Iron–sulfur clusters are ubiquitous in biology and function in electron transfer and catalysis. They are assembled from iron and cysteine sulfur on protein scaffolds. Iron is typically stored as iron oxyhydroxide, ferrihydrite, encapsulated in 12 nm shells of ferritin, which buffers cellular iron availability. Here we have characterized IssA, a protein that stores iron and sulfur as thioferrate, an inorganic anionic polymer previously unknown in biology. IssA forms nanoparticles reaching 300 nm in diameter and is the largest natural metalloprotein complex known. It is a member of a widely distributed protein family that includes nitrogenase maturation factors, NifB and NifX. IssA nanoparticles are visible by electron microscopy as electron-dense bodies in the cytoplasm. Purified nanoparticles appear to be generated from 20 nm units containing ∼6,400 Fe atoms and ∼170 IssA monomers. In support of roles in both iron–sulfur storage and cluster biosynthesis, IssA reconstitutes the [4Fe-4S] cluster in ferredoxin in vitro.

Suggested Citation

  • Brian J. Vaccaro & Sonya M. Clarkson & James F. Holden & Dong-Woo Lee & Chang-Hao Wu & Farris L. Poole II & Julien J. H. Cotelesage & Mark J. Hackett & Sahel Mohebbi & Jingchuan Sun & Huilin Li & Mich, 2017. "Biological iron-sulfur storage in a thioferrate-protein nanoparticle," Nature Communications, Nature, vol. 8(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms16110
    DOI: 10.1038/ncomms16110
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