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Evolutionary conservation and in vitro reconstitution of microsporidian iron–sulfur cluster biosynthesis

Author

Listed:
  • Sven-A. Freibert

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität)

  • Alina V. Goldberg

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Christian Hacker

    (School of Medicine, University of St Andrews
    Bioimaging Centre, College of Life and Environmental Sciences, University of Exeter)

  • Sabine Molik

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität)

  • Paul Dean

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Tom A. Williams

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Sirintra Nakjang

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Shaojun Long

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Kacper Sendra

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Eckhard Bill

    (Max-Planck-Institut für Bioanorganische Chemie)

  • Eva Heinz

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Robert P. Hirt

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • John M Lucocq

    (School of Medicine, University of St Andrews)

  • T. Martin Embley

    (Institute for Cell and Molecular Biosciences, University of Newcastle)

  • Roland Lill

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität
    LOEWE Zentrum für Synthetische Mikrobiologie SynMikro)

Abstract

Microsporidians are obligate intracellular parasites that have minimized their genome content and sub-cellular structures by reductive evolution. Here, we demonstrate that cristae-deficient mitochondria (mitosomes) of Trachipleistophora hominis are the functional site of iron–sulfur cluster (ISC) assembly, which we suggest is the essential task of these organelles. Cell fractionation, fluorescence imaging and immunoelectron microscopy demonstrate that mitosomes contain a complete pathway for [2Fe–2S] cluster biosynthesis that we biochemically reconstituted using purified mitosomal ISC proteins. The T. hominis cytosolic iron–sulfur protein assembly (CIA) pathway includes the essential Cfd1–Nbp35 scaffold complex that assembles a [4Fe–4S] cluster as shown by spectroscopic methods in vitro. Phylogenetic analyses reveal that the ISC and CIA pathways are predominantly bacterial, but their cytosolic and nuclear target Fe/S proteins are mainly archaeal. This mixed evolutionary history of Fe/S-related proteins and pathways, and their strong conservation among highly reduced parasites, provides compelling evidence for the ancient chimeric ancestry of eukaryotes.

Suggested Citation

  • Sven-A. Freibert & Alina V. Goldberg & Christian Hacker & Sabine Molik & Paul Dean & Tom A. Williams & Sirintra Nakjang & Shaojun Long & Kacper Sendra & Eckhard Bill & Eva Heinz & Robert P. Hirt & Joh, 2017. "Evolutionary conservation and in vitro reconstitution of microsporidian iron–sulfur cluster biosynthesis," Nature Communications, Nature, vol. 8(1), pages 1-12, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms13932
    DOI: 10.1038/ncomms13932
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