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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F17%3A00479062" target="_blank" >RIV/60077344:_____/17:00479062 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/17:43895454

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.molbiopara.2017.03.009" target="_blank" >http://dx.doi.org/10.1016/j.molbiopara.2017.03.009</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.molbiopara.2017.03.009" target="_blank" >10.1016/j.molbiopara.2017.03.009</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular and Biochemical Parasitology

ISSN

0166-6851

e-ISSN

—

Svazek periodika

214

Číslo periodika v rámci svazku

JUN

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

5

Strana od-do

47-51

Kód UT WoS článku

000404795200006

EID výsledku v databázi Scopus

2-s2.0-85017144077