The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone

Haindrich, Alexander C.; Boudova, M.; Vancová, Marie; Peña-Diaz, Priscila; Horáková, Eva; Lukeš, Julius

doi:https://dx.doi.org/10.1016/j.molbiopara.2017.03.009

Number of the records: 1

The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone

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SYSNO ASEP	0479062
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone
Author(s)	Haindrich, Alexander C. (BC-A) Boudova, M. (CZ) Vancová, Marie (BC-A)_{RID, ORCID} Peña-Diaz, Priscila (BC-A)_{ORCID, RID} Horáková, Eva (BC-A)_{RID, ORCID} Lukeš, Julius (BC-A)_{RID, ORCID}
Number of authors	6
Source Title	Molecular and Biochemical Parasitology. - : Elsevier - ISSN 0166-6851 Roč. 214, JUN (2017), s. 47-51
Number of pages	5 s.
Publication form	Print - P
Language	eng - English
Country	NL - Netherlands
Keywords	Trypanosoma ; Erv1 ; Fe-S cluster assembly ; mitochondrion
Subject RIV	EB - Genetics ; Molecular Biology
OECD category	Biochemistry and molecular biology
R&D Projects	GA15-21974S GA ČR - Czech Science Foundation (CSF)
	GA16-18699S GA ČR - Czech Science Foundation (CSF)
Institutional support	BC-A - RVO:60077344
UT WOS	000404795200006
EID SCOPUS	85017144077
DOI	10.1016/j.molbiopara.2017.03.009
Annotation	Sulfhydryl oxidase Erv1 is a ubiquitous and conserved protein of the mitochondrial intermembrane space that plays a role in the transport of small sulfur-containing proteins. In higher eukaryotes, Erv1 interacts with the mitochondrial import protein Mia40. However, Trypanosoma brucei lacks an obvious Mia40 homologue in its genome. Here we show by tandem affinity purification and mass spectrometry that in this excavate protist, Erv1 functions without a Mia40 homologue and most likely any other interaction partner. Down-regulation of TbErvl caused a reduction of the mitochondrial membrane potential already within 24 h to less than 50% when compared with control cells. The depletion of TbErv1 was accompanied by accumulation of trCOIV precursor, with a concomitant reduction of aconitase activity both in the cytosol and mitochondrion. Overall, TbErv1 seems to have a role in the mitochondrial translocation and Fe-S cluster assembly in the organelle. (C) 2017 Elsevier B.V. All rights reserved.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2018

Number of the records: 1