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Lookup NU author(s): Dr Alina Goldberg Cavalleri, Dr Paul Dean, Dr Tom Williams, Dr Sirintra Nakjang, Dr Shaojun Long, Dr Kacper Sendra, Dr Eva Heinz, Professor Robert HirtORCiD, Emeritus Professor T. Martin Embley FMedSci FRSORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
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.
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
Date deposited: 01/03/2017
ISSN (electronic): 2041-1723
Publisher: Nature Publishing Group
URL: https://doi.org/10.1038/ncomms13932
DOI: 10.1038/ncomms13932
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