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research
Bacterial-type oxygen detoxification and iron-sulfur cluster assembly in amoebal relict mitochondria.
Authors
Aguilera
Ali
+53 more
Arias
Bakatselou
Bakatselou
Beinert
Beinert
Bradford
Chan
Choi
Clark
Coulter
Coulter
Craig
Davis
Diamond
Dolezal
Embley
Embley
Embley
Esser
Frazzon
Gerber
Ghosh
Gill
Goldberg
Jin
Katinka
Kurland
León-Avila
Lill
Lill
Loftus
Loiseau
Lucattini
Mahendrasingam
Morrison
Müller
Müller
Outten
Pütz
Rees
Reeves
Regoes
Stanley
Suták
Takahashi
Tovar
Tovar
Tovar
van der Giezen
van der Giezen
van der Giezen
Vicente
Weinberg
Publication date
6 June 2013
Publisher
'Wiley'
Doi
Cite
Abstract
addresses: School of Biological Sciences, Royal Holloway University of London, Egham TW20 0EX, UK.types: Journal Article; Research Support, Non-U.S. Gov'tOnline open article. This is a copy of an article published in Cellular Microbiology © 2009 Blackwell Publishing Ltd. Cellular Microbiology is available online at: http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-5822The assembly of vital reactive iron-sulfur (Fe-S) cofactors in eukaryotes is mediated by proteins inherited from the original mitochondrial endosymbiont. Uniquely among eukaryotes, however, Entamoeba and Mastigamoeba lack such mitochondrial-type Fe-S cluster assembly proteins and possess instead an analogous bacterial-type system acquired by lateral gene transfer. Here we demonstrate, using immunomicroscopy and biochemical methods, that beyond their predicted cytosolic distribution the bacterial-type Fe-S cluster assembly proteins NifS and NifU have been recruited to function within the relict mitochondrial organelles (mitosomes) of Entamoeba histolytica. Both Nif proteins are 10-fold more concentrated within mitosomes compared with their cytosolic distribution suggesting that active Fe-S protein maturation occurs in these organelles. Quantitative immunoelectron microscopy showed that amoebal mitosomes are minute but highly abundant cellular structures that occupy up to 2% of the total cell volume. In addition, protein colocalization studies allowed identification of the amoebal hydroperoxide detoxification enzyme rubrerythrin as a mitosomal protein. This protein contains functional Fe-S centres and exhibits peroxidase activity in vitro. Our findings demonstrate the role of analogous protein replacement in mitochondrial organelle evolution and suggest that the relict mitochondrial organelles of Entamoeba are important sites of metabolic activity that function in Fe-S protein-mediated oxygen detoxification
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Last time updated on 26/03/2019
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Open Research Exeter
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oai:ore.exeter.ac.uk:10871/989...
Last time updated on 06/08/2013