High Osmolarity Environments Activate the Mitochondrial Alternative Oxidase in Debaryomyces Hansenii.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28060946.
- Also identified by DOI 10.1371/journal.pone.0169621 and PMC identifier 5218487.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The oleaginous yeast Debaryomyces hansenii is a good model to understand molecular mechanisms involved in halotolerance because of its impressive ability to survive under a wide range of salt concentrations. Several cellular adaptations are implicated in this response, including the presence of a cyanide-insensitive ubiquinol oxidase (Aox). This protein, which is present in several taxonomical orders, has been related to different stress responses. However, little is known about its role in mitochondria during transitions from low to high saline environments. In this report, we analyze the effects of Aox in shifts from low to high salt concentrations in the culture media. At early stages of a salt insult, we observed that this protein prevents the overflow of electrons on the mitochondrial respiratory chain, thus, decreasing the production of reactive oxygen species. Interestingly, in the presence of high osmolite concentrations, Aox activity is able to sustain a stable membrane potential when coupled to complex I, despite a compromised cytochrome pathway. Taken together, our results suggest that under high osmolarity conditions Aox plays a critical role regulating mitochondrial physiology.
Medical subject headings
- Ascomycota
- Mitochondria
- Mitochondrial Proteins
- Osmolar Concentration
- Oxidoreductases
- Plant Proteins