A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

0537478 - BC 2021 RIV US eng J - Journal Article
Hammond, Michael John - Nenarokova, Anna - Butenko, Anzhelika - Zoltner, M. - Dobáková, Eva - Field, Mark Christian - Lukeš, Julius
A Uniquely Complex Mitochondrial Proteome from Euglena gracilis.
Molecular Biology and Evolution. Roč. 37, č. 8 (2020), s. 2173-2191. ISSN 0737-4038. E-ISSN 1537-1719
R&D Projects: GA MŠMT(CZ) LL1601; GA ČR(CZ) GA18-15962S; GA MŠMT(CZ) EF16_019/0000759
EU Projects: Wellcome Trust(GB) 204697/Z/16/Z
Institutional support: RVO:60077344
Keywords : wax ester fermentation * trypanosoma-brucei * comprehensive analysis * alternative oxidase * micos complex * proteins * rna * biogenesis * genome * prediction * mitochondria * proteome * protist * Euglenozoa * Euglena gracilis
OECD category: Genetics and heredity (medical genetics to be 3)
Impact factor: 16.240, year: 2020
Method of publishing: Open access
https://academic.oup.com/mbe/article/37/8/2173/5803078

Euglena gracilis is ametabolically flexible, photosynthetic, and adaptable free-living protist of considerable environmental importance and biotechnological value. By label-free liquid chromatography tandem mass spectrometry, a total of 1,786 proteins were identified from the E. gracilis purified mitochondria, representing one of the largest mitochondrial proteomes so far described. Despite this apparent complexity, protein machinery responsible for the extensive RNA editing, splicing, and processing in the sister clades diplonemids and kinetoplastids is absent. This strongly suggests that the complex mechanisms of mitochondrial gene expression in diplonemids and kinetoplastids occurred late in euglenozoan evolution, arising independently. By contrast, the alternative oxidase pathway and numerous ribosomal subunits presumed to be specific for parasitic trypanosomes are present in E. gracilis. We investigated the evolution of unexplored protein families, including import complexes, cristae formation proteins, and translation termination factors, as well as canonical and unique metabolic pathways. We additionally compare this mitoproteome with the transcriptome of Eutreptiella gymnastica, illuminating conserved features of Euglenida mitochondria as well as those exclusive to E. gracilis. This is the first mitochondrial proteome of a free-living protist from the Excavata and one of few available for protists as a whole. This study alters our views of the evolution of the mitochondrion and indicates early emergence of complexity within euglenozoan mitochondria, independent of parasitism.
Permanent Link: http://hdl.handle.net/11104/0315270