Subunit composition of mitochondrial dehydrogenase complexes in diplonemid flagellates
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
37451476
DOI
10.1016/j.bbagen.2023.130419
PII: S0304-4165(23)00117-4
Knihovny.cz E-zdroje
- Klíčová slova
- Dehydrogenase complexes, Diplonema papillatum, Diplonemids, Evolution, Mitochondrion, Protist,
- MeSH
- ketoglutarátdehydrogenasový komplex metabolismus MeSH
- mitochondrie * metabolismus MeSH
- multienzymové komplexy metabolismus MeSH
- pyruvátdehydrogenasový komplex * metabolismus MeSH
- pyruváty metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- ketoglutarátdehydrogenasový komplex MeSH
- multienzymové komplexy MeSH
- pyruvátdehydrogenasový komplex * MeSH
- pyruváty MeSH
In eukaryotes, pyruvate, a key metabolite produced by glycolysis, is converted by a tripartite mitochondrial pyruvate dehydrogenase (PDH) complex to acetyl-coenzyme A, which is fed into the tricarboxylic acid cycle. Two additional enzyme complexes with analogous composition catalyze similar oxidative decarboxylation reactions albeit using different substrates, the branched-chain ketoacid dehydrogenase (BCKDH) complex and the 2-oxoglutarate dehydrogenase (OGDH) complex. Comparative transcriptome analyses of diplonemids, one of the most abundant and diverse groups of oceanic protists, indicate that the conventional E1, E2, and E3 subunits of the PDH complex are lacking. E1 was apparently replaced in the euglenozoan ancestor of diplonemids by an AceE protein of archaeal type, a substitution that we also document in dinoflagellates. Here, we demonstrate that the mitochondrion of the model diplonemid Paradiplonema papillatum displays pyruvate and 2-oxoglutarate dehydrogenase activities. Protein mass spectrometry of mitochondria reveal that the AceE protein is as abundant as the E1 subunit of BCKDH. This corroborates the view that the AceE subunit is a functional component of the PDH complex. We hypothesize that by acquiring AceE, the diplonemid ancestor not only lost the eukaryotic-type E1, but also the E2 and E3 subunits of the PDH complex, which are present in other euglenozoans. We posit that the PDH activity in diplonemids seems to be carried out by a complex, in which the AceE protein partners with the E2 and E3 subunits from BCKDH and/or OGDH.
e Duve Institute Université Catholique de Louvain Brussels Belgium
Faculty of Natural Sciences Comenius University Bratislava Slovakia
Institute of Chemistry Slovak Academy of Sciences Bratislava Slovakia
Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czech Republic
Citace poskytuje Crossref.org
Genetic Manipulation of Paradiplonema papillatum
