-
Je něco špatně v tomto záznamu ?
The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone
AC. Haindrich, M. Boudová, M. Vancová, PP. Diaz, E. Horáková, J. Lukeš,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články
- MeSH
- hmotnostní spektrometrie MeSH
- mapování interakce mezi proteiny MeSH
- mitochondrie enzymologie metabolismus MeSH
- oxidoreduktasy metabolismus MeSH
- proteiny obsahující železo a síru metabolismus MeSH
- protozoální proteiny metabolismus MeSH
- Trypanosoma brucei brucei enzymologie metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
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 TbErv1 caused a reduction of the mitochondrial membrane potential already within 24h 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.
Canadian Institute for Advanced Research Toronto Ontario M5G 1Z8 Canada
Faculty of Sciences University of South Bohemia 37005 České Budějovice Czech Republic
Institute of Parasitology Biology Centre 37005 České Budějovice Czech Republic
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc18010707
- 003
- CZ-PrNML
- 005
- 20180420093927.0
- 007
- ta
- 008
- 180404s2017 ne f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1016/j.molbiopara.2017.03.009 $2 doi
- 035 __
- $a (PubMed)28366668
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $a Haindrich, Alexander C $u Institute of Parasitology, Biology Centre, 37005 České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, 37005 České Budějovice (Budweis), Czech Republic.
- 245 14
- $a The intermembrane space protein Erv1 of Trypanosoma brucei is essential for mitochondrial Fe-S cluster assembly and operates alone / $c AC. Haindrich, M. Boudová, M. Vancová, PP. Diaz, E. Horáková, J. Lukeš,
- 520 9_
- $a 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 TbErv1 caused a reduction of the mitochondrial membrane potential already within 24h 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.
- 650 _2
- $a proteiny obsahující železo a síru $x metabolismus $7 D007506
- 650 _2
- $a hmotnostní spektrometrie $7 D013058
- 650 _2
- $a mitochondrie $x enzymologie $x metabolismus $7 D008928
- 650 _2
- $a oxidoreduktasy $x metabolismus $7 D010088
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a mapování interakce mezi proteiny $7 D025941
- 650 _2
- $a protozoální proteiny $x metabolismus $7 D015800
- 650 _2
- $a Trypanosoma brucei brucei $x enzymologie $x metabolismus $7 D014346
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Boudová, Michala $u Faculty of Sciences, University of South Bohemia, 37005 České Budějovice (Budweis), Czech Republic.
- 700 1_
- $a Vancová, Marie $u Institute of Parasitology, Biology Centre, 37005 České Budějovice (Budweis), Czech Republic.
- 700 1_
- $a Diaz, Priscila Peña $u Institute of Parasitology, Biology Centre, 37005 České Budějovice (Budweis), Czech Republic.
- 700 1_
- $a Horáková, Eva $u Institute of Parasitology, Biology Centre, 37005 České Budějovice (Budweis), Czech Republic.
- 700 1_
- $a Lukeš, Julius $u Institute of Parasitology, Biology Centre, 37005 České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, 37005 České Budějovice (Budweis), Czech Republic; Canadian Institute for Advanced Research, Toronto, Ontario M5G 1Z8, Canada. Electronic address: jula@paru.cas.cz.
- 773 0_
- $w MED00003384 $t Molecular and biochemical parasitology $x 1872-9428 $g Roč. 214, č. - (2017), s. 47-51
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/28366668 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20180404 $b ABA008
- 991 __
- $a 20180420094030 $b ABA008
- 999 __
- $a ok $b bmc $g 1288192 $s 1007519
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2017 $b 214 $c - $d 47-51 $e 20170331 $i 1872-9428 $m Molecular and biochemical parasitology $n Mol Biochem Parasitol $x MED00003384
- LZP __
- $a Pubmed-20180404
