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The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo
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SYSNO ASEP 0557404 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo Author(s) Kaurov, Iosif (BC-A)
Heller, Jiří (BC-A)
Deisenhammer, S. (CZ)
Potěšil, D. (CZ)
Zdráhal, Z. (CZ)
Hashimi, Hassan (BC-A) RID, ORCIDNumber of authors 6 Article number 111463 Source Title Molecular and Biochemical Parasitology. - : Elsevier - ISSN 0166-6851
Roč. 248, MAR (2022)Number of pages 10 s. Publication form Online - E Language eng - English Country NL - Netherlands Keywords intermembrane space ; bond formation ; mia pathway ; redox properties ; protein import ; relay system ; mitochondrial ; identification ; evolution ; oxidoreductase ; Trypanosoma ; Mitochondrion ; micos ; Protein import ; Intermembrane space ; Oxidative folding Subject RIV EA - Cell Biology OECD category Cell biology R&D Projects GA20-23513S GA ČR - Czech Science Foundation (CSF) EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BC-A - RVO:60077344 UT WOS 000787886300003 EID SCOPUS 85124461383 DOI 10.1016/j.molbiopara.2022.111463 Annotation The mitochondrial protein import machinery of trypanosomatids is highly divergent from that of the well-studied models such as baker's yeast. A notable example is that the central catalyst of the mitochondrial intermembrane space import and assembly pathway (MIA), named Mia40, is missing in trypanosomatids. Mia40 works in a two-step process. First it recognizes by direct binding reduced MIA substrate proteins and then catalyzes their oxidative folding to produce intramolecular disulfide bridges. It was recently proposed that a thioredoxin-like subunit of the trypanosomal mitochondrial contact site and cristae organizing system (MICOS) called TbMic20 may be the Mia40 replacement. Our study performed on procyclic stage of the parasite revealed that each of the two cysteines in TbMic20's active site is essential for the stability of MIA substrate proteins although they do not form a disulfide bridge in vivo. The two cysteines of Mia40 & PRIME,s active site form an intramolecular di-sulfide bridge at steady state, which is a prerequisite for its oxidative folding of MIA substrates. Thus, we conclude that TbMic20 is unlikely to represent a bona fide Mia40 replacement and plays a still unresolved role in the stability and/or import of MIA substrates in trypanosomatids. Despite this, the effect of TbMic20 depletion and mutation indicates that the trypanosomal MICOS complex still plays a vital role in the maturation and/or stability of proteins imported by the MIA pathway. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2023 Electronic address https://www.sciencedirect.com/science/article/pii/S0166685122000172?via%3Dihub
Number of the records: 1