ATP regulates the activity of an alternative oxidase in Trypanosoma brucei

Author(s)

Luevano-Martinez, Luis Alberto ^[1] ; Girard, Richard M. B. M. ^[1] ; Alencar, Mayke Bezerra ^[1] ; Silber, Ariel Mariano ^[1]

Affiliation

^[1] Univ Sao Paulo, Inst Biomed Sci, Dept Parasitol, Lab Biochem Tryps LaBTryps, Sao Paulo - Brazil

• Document type: Journal article
• Source: FEBS Letters; v. 594, n. 13, p. 2150-2158, JUL 2020.
• Web of Science Citations: 3

Abstract

The reduced mitochondrial respiratory chain from the bloodstream forms of Trypanosoma brucei is composed of only a membrane-bound glycerol-3-phosphate dehydrogenase and an alternative oxidase. Since these enzymes are not proton pumps, their functions are restricted to the maintenance of the redox balance in the glycosome by means of the dihydroxyacetone phosphate/glycerol-3-phosphate shuttle. Additionally, an F1Fo-ATP synthase functions as an ATP-hydrolysing enzyme to establish the proton motive force necessary to maintain the basic functions of mitochondria. In this report, we studied the interplay between the alternative oxidase and ATP synthase, and we found that, in addition to its role as a proton pump, ATP synthase contributes to maintain safe levels of ATP to prevent the inhibition of the alternative oxidase by ATP. (AU)

• FAPESP's process: 16/06034-2 - The biological role of amino acids and their metabolites in Trypanosoma cruzi
• Grantee: Ariel Mariano Silber
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 16/12999-0 - Evolution of the cardiolipin biosynthetic pathway: biochemical implications for the evolution of the Eukarya domain
• Grantee: Luis Alberto Luevano Martinez
• Support Opportunities: Research Grants - Young Investigators Grants