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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, 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.

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

Date deposited: 01/03/2017

ISSN (electronic): 2041-1723

Publisher: Nature Publishing Group


DOI: 10.1038/ncomms13932


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Funder referenceFunder name
LOEWE program of state Hessen
Marie Curie Postdoctoral Fellowships
Max-Planck Gesellschaft
von Behring-Rontgen Stiftung
045404Wellcome Trust Programme Grant
ERC-2010-AdG-268701European Research Council Advanced Investigator Grant
GRK 1216Deutsche Forschungsgemeinschaft
LI 415/5Deutsche Forschungsgemeinschaft
SFB 593Deutsche Forschungsgemeinschaft
SFB 987Deutsche Forschungsgemeinschaft
SFB 593, SFB 987, GRK 1216, LI 415/5
Wellcome Trust Programme Grant (Number 045404)