Subunit composition of mitochondrial dehydrogenase complexes in diplonemid flagellates.

Autor: Záhonová K; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic; Life Science Research Centre, Faculty of Science, University of Ostrava, Ostrava, Czech Republic; Department of Parasitology, Faculty of Science, Charles University, BIOCEV, Vestec, Czech Republic; Division of Infectious Diseases, Department of Medicine, University of Alberta, Edmonton, Canada., Valach M; Department of Biochemistry and Robert-Cedergren Centre for Bioinformatics and Genomics, Université de Montréal, Montreal, Canada., Tripathi P; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic., Benz C; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic., Opperdoes FR; de Duve Institute, Université Catholique de Louvain, Brussels, Belgium., Barath P; Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia; Medirex Group Academy, Nitra, Slovakia., Lukáčová V; Medirex Group Academy, Nitra, Slovakia., Danchenko M; Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia., Faktorová D; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic., Horváth A; Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia., Burger G; Department of Biochemistry and Robert-Cedergren Centre for Bioinformatics and Genomics, Université de Montréal, Montreal, Canada., Lukeš J; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic. Electronic address: jula@paru.cas.cz., Škodová-Sveráková I; Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic; Life Science Research Centre, Faculty of Science, University of Ostrava, Ostrava, Czech Republic; Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia. Electronic address: skodovaister@gmail.com.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. General subjects [Biochim Biophys Acta Gen Subj] 2023 Sep; Vol. 1867 (9), pp. 130419. Date of Electronic Publication: 2023 Jul 13.
DOI: 10.1016/j.bbagen.2023.130419
Abstrakt: 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.
Competing Interests: Declaration of Competing Interest The authors declare that they have no conflicts of interest with the contents of this article.
(Copyright © 2023. Published by Elsevier B.V.)
Databáze: MEDLINE
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