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

Lookup NU author(s): Dr Alina Goldberg Cavalleri, Dr Paul Dean, Dr Tom Williams, Dr Sirintra Nakjang, Dr Shaojun Long, Kacper Sendra, Dr Eva Heinz, Professor Robert Hirt, Professor T. Martin Embley

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


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.


Publication metadata

Author(s): Freibert SA, Goldberg AV, Hacker C, Molik S, Dean P, Williams TA, Nakjang S, Long SJ, Sendra K, Bill E, Heinz E, Hirt RP, Lucocq JM, Embley TM, Lill R

Publication type: Article

Publication status: Published

Journal: Nature Communcations

Year: 2017

Volume: 8

Online publication date: 04/01/2017

Acceptance date: 14/11/2016

ISSN (electronic): 2041-1723

Publisher: Nature Publishing Group

URL: https://doi.org/10.1038/ncomms13932

DOI: 10.1038/ncomms13932


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