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Updated: Aug 22, 2025

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
Reduced mitochondria provide an essential function for the cytosolic methionine cycle
Justyna Zítek1, Zoltán Füssy1, Sebastian C Treitli1
1Charles University, Faculty of Science, Department of Parasitology, BIOCEV, Vestec 252 50, Czech Republic.
Abstract:
The loss of mitochondria in oxymonad protists has been associated with the redirection of the essential Fe-S cluster assembly to the cytosol. Yet as our knowledge of diverse free-living protists broadens, the list of functions of their mitochondrial-related organelles (MROs) expands. We revealed another such function in the closest oxymonad relative, Paratrimastix pyriformis, after we solved the proteome of its MRO with high accuracy, using localization of organelle proteins by isotope tagging (LOPIT). The newly assigned enzymes connect to the glycine cleavage system (GCS) and produce folate derivatives with one-carbon units and formate. These are likely to be used by the cytosolic methionine cycle involved in S-adenosyl methionine recycling. The data provide consistency with the presence of the GCS in MROs of free-living species and its absence in most endobionts, which typically lose the methionine cycle and, in the case of oxymonads, the mitochondria.
Insights
Mitochondrial-related organelles in protists perform new functions. In Paratrimastix pyriformis, these organelles host the glycine cleavage system, supplying one-carbon units for essential cellular processes.
Area of Science:
- Cell Biology
- Protistology
- Biochemistry
Background:
- Mitochondria are often lost in oxymonad protists, with Fe-S cluster assembly shifting to the cytosol.
- The functions of mitochondrial-related organelles (MROs) in diverse protists are increasingly recognized.
Purpose of the Study:
- To investigate the proteome of the MRO in Paratrimastix pyriformis, an oxymonad relative.
- To identify novel functions of MROs in free-living protists.
Main Methods:
- High-accuracy proteome analysis of MROs using Localization of Organelle Proteins by Isotope Tagging (LOPIT).
Main Results:
- Identified enzymes linked to the glycine cleavage system (GCS) within the MRO.
- These enzymes produce folate derivatives and formate, crucial for one-carbon metabolism.
- These products likely support the cytosolic methionine cycle and S-adenosyl methionine recycling.
Conclusions:
- The MRO in P. pyriformis hosts the glycine cleavage system, a previously unrecognized function.
- This finding supports the presence of GCS in MROs of free-living protists.
- The absence of GCS in endosymbiotic species correlates with the loss of the methionine cycle and mitochondria.
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