Počet záznamů: 1
The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone
- 1. 0479062 - BC-A 2018 RIV NL eng J - Článek v odborném periodiku
Haindrich, Alexander C. - Boudova, M. - Vancová, Marie - Peña-Diaz, Priscila - Horáková, Eva - Lukeš, Julius
The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone.
Molecular and Biochemical Parasitology. Roč. 214, JUN (2017), s. 47-51. ISSN 0166-6851
Grant CEP: GA ČR GA15-21974S; GA ČR(CZ) GA16-18699S
Institucionální podpora: RVO:60077344
Klíčová slova: Trypanosoma * Erv1 * Fe-S cluster assembly * mitochondrion
Kód oboru RIV: EB - Genetika a molekulární biologie
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 1.744, rok: 2017
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.
Trvalý link: http://hdl.handle.net/11104/0275085