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A mitochondrion-free eukaryote contains proteins capable of import into an exogenous mitochondrion-related organelle
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SYSNO ASEP 0567556 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title A mitochondrion-free eukaryote contains proteins capable of import into an exogenous mitochondrion-related organelle Author(s) Fang, Y. K. (CZ)
Vaitová, Zuzana (UOCHB-X)
Hampl, V. (CZ)Article number 220238 Source Title Open Biology. - : Royal Society Publishing
Roč. 13, č. 1 (2023)Number of pages 9 s. Language eng - English Country GB - United Kingdom Keywords mitochondrion-free eukaryote ; hydrogenosome ; protein import ; evolution of protein targeting OECD category Biochemistry and molecular biology Research Infrastructure Czech-BioImaging II - 90129 - Ústav molekulární genetiky AV ČR, v. v. i. Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 000912067900005 EID SCOPUS 85146101955 DOI 10.1098/rsob.220238 Annotation The endobiotic flagellate Monocercomonoides exilis is the only known eukaryote to have lost mitochondria and all its associated proteins in its evolutionary past. This final stage of the mitochondrial evolutionary pathway may serve as a model to explain events at their very beginning such as the initiation of protein import. We have assessed the capability of proteins from this eukaryote to enter emerging mitochondria using a specifically designed in vitro assay. Hydrogenosomes (reduced mitochondria) of Trichomonas vaginalis were incubated with a soluble protein pool derived from a cytosolic fraction of M. exilis, and proteins entering hydrogenosomes were subsequently detected by mass spectrometry. The assay detected 19 specifically and reproducibly imported proteins, and in 14 cases the import was confirmed by the overexpression of their tagged version in T. vaginalis. In most cases, only a small portion of the signal reached the hydrogenosomes, suggesting specific but inefficient transport. Most of these proteins represent enzymes of carbon metabolism, and none exhibited clear signatures of proteins targeted to hydrogenosomes or mitochondria, which is consistent with their inefficient import. The observed phenomenon may resemble a primaeval type of protein import which might play a role in the establishment of the organelle and shaping of its proteome in the initial stages of endosymbiosis. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2024 Electronic address https://doi.org/10.1098/rsob.220238
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