The mitochondrial phosphate carrier TbMCP11 is essential for mitochondrial function in the procyclic form of Trypanosoma brucei
Gao, Fei; Voncken, Frank; Colasante, Claudia
Conserved amongst all eukaryotes is a family of mitochondrial carrier proteins (SLC25A) responsible for the import of various solutes across the inner mitochondrial membrane. We previously reported that the human parasite Trypanosoma brucei possesses 26 SLC25A proteins (TbMCPs) amongst which two, TbMCP11 and TbMCP8, were predicted to function as phosphate importers. The transport of inorganic phosphate into the mitochondrion is a prerequisite to drive ATP synthesis by substrate level and oxidative phosphorylation and thus crucial for cell viability. In this paper we describe the functional characterization of TbMCP11. In procyclic form T. brucei, the RNAi of TbMCP11 blocked ATP synthesis on mitochondrial substrates, caused a drop of the mitochondrial oxygen consumption and drastically reduced cell viability. The functional complementation in yeast and mitochondrial swelling experiments suggested a role for TbMCP11 as inorganic phosphate carrier. Interestingly, procyclic form T. brucei cells in which TbMCP11 was depleted displayed an inability to either replicate or divide the kinetoplast DNA, which resulted in a severe cytokinesis defect.
Gao, F., Voncken, F., & Colasante, C. (2020). The mitochondrial phosphate carrier TbMCP11 is essential for mitochondrial function in the procyclic form of Trypanosoma brucei. Molecular and Biochemical Parasitology, 237, https://doi.org/10.1016/j.molbiopara.2020.111275
|Journal Article Type||Article|
|Acceptance Date||Mar 24, 2020|
|Online Publication Date||Apr 27, 2020|
|Deposit Date||May 1, 2020|
|Publicly Available Date||Apr 28, 2021|
|Journal||Molecular and Biochemical Parasitology|
|Peer Reviewed||Peer Reviewed|
|Keywords||Mitochondrial carrier family; Energy metabolism; Trypanosoma brucei; Cytokinesis; Phosphate transport; Mitochondrial membrane potential|
This file is under embargo until Apr 28, 2021 due to copyright reasons.
Contact F.Voncken@hull.ac.uk to request a copy for personal use.
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