A Uniquely Complex Mitochondrial Proteome from Euglena gracilis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F20%3AA21027BI" target="_blank" >RIV/61988987:17310/20:A21027BI - isvavai.cz</a>
Alternative codes found
RIV/60077344:_____/20:00537478 RIV/60076658:12310/20:43901108 RIV/00216208:11310/20:10418110
Result on the web
<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7403612/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7403612/</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/molbev/msaa061" target="_blank" >10.1093/molbev/msaa061</a>
Alternative languages
Result language
angličtina
Original language name
A Uniquely Complex Mitochondrial Proteome from Euglena gracilis
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10601 - Cell biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
MOL BIOL EVOL
ISSN
0737-4038
e-ISSN
1537-1719
Volume of the periodical
37
Issue of the periodical within the volume
8
Country of publishing house
GB - UNITED KINGDOM
Number of pages
19
Pages from-to
2173-2191
UT code for WoS article
000574381000002
EID of the result in the Scopus database
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