Difference between revisions of "Garcia-Neto 2017 PLOS ONE"
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|journal=PLOS ONE | |journal=PLOS ONE | ||
|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. | |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. | ||
|editor=[[Kandolf G]], | |||
|mipnetlab=BR Sao Paulo Kowaltowski AJ | |mipnetlab=BR Sao Paulo Kowaltowski AJ | ||
}} | }} | ||
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|area=Respiration, Comparative MiP;environmental MiP | |area=Respiration, Comparative MiP;environmental MiP | ||
|organism=Fungi | |organism=Fungi | ||
|preparations=Isolated mitochondria | |||
|couplingstates=ETS | |||
|pathways=N, S, CIV, ROX | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=Labels, | |additional=Labels, 2017-02, | ||
}} | }} | ||
Revision as of 11:13, 21 February 2017
| Garcia-Neto W, Cabrera-Orefice A, Uribe-Carvajal S, Kowaltowski AJ, Alberto Luévano-Martínez L (2017) High osmolarity environments activate the mitochondrial alternative oxidase in Debaryomyces Hansenii. PLOS ONE 12:e0169621. |
Garcia-Neto W, Cabrera-Orefice A, Uribe-Carvajal S, Kowaltowski AJ, Luevano-Martinez AL (2017) PLOS ONE
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.
• Bioblast editor: Kandolf G • O2k-Network Lab: BR Sao Paulo Kowaltowski AJ
Labels: MiParea: Respiration, Comparative MiP;environmental MiP
Organism: Fungi
Preparation: Isolated mitochondria
Coupling state: ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.
Pathway: N, S, CIV, ROX
HRR: Oxygraph-2k
Labels, 2017-02
