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Characterization and biological role of Cysteine catabolism in Trypanosoma cruzi.
The conversion of Cysteine to Pyruvate can be carried out by two enzymes, a broad-spectrum substrate Aspartate aminotransferase (ASAT), which includes Cys among them, and a Mercaptopyruvate Sulfotransferase (MPST). Due to their characteristics, ASAT of T. cruzi are potential candidates to catalyze the Cystein deamination. However, despite a putative sequence for these enzymes in the T. cruzi genome, there is currently no literature data showing this pathway. The goal of this project is to confirm this "direct" pathway for Pyruvate production from cystein, and the possible existence of a dual connection between Serine and Cystein: through the enzyme cystathionine--synthase, Serine could be converted to Cystein (and subsequently to Pyruvate) or conversely, through the enzyme Cystein--lyase (CGL) and the reverse action of cystathionine--synthase (CBS), Cystein could provide Serine, which could also provide Pyr through a Serine dehydrogenase. The reason for the co-existence of both pathways is not clear, as it seems that both primarily function to provide Pyruvate, one using Ser as intermediates and the other using Cystein. The goal of this project is to explore these pathweays using methods in enzymology, biochemistry, metabolomics, bioenergetics and gene edition by CRISPR/Cas9.
Deadline for applications: April 8th., 2024
For applying send:
Motivation Letter
CV
Two recommendation letters