Cloning of metacaspase YCA1 with N-terminal deletion

• Grant number: 18/16761-4
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Start date: November 01, 2018
• End date: October 31, 2019
• Field of knowledge: Biological Sciences - Biochemistry - Molecular Biology
• Principal Investigator: Mauricio Ferreira Marcondes Machado
• Grantee: Isabela Ramos Sales Prado
• Host Institution: Pró-Reitoria Acadêmica. Universidade de Mogi das Cruzes (UMC). Campus da Sede Mogi das Cruzes. Mogi das Cruzes , SP, Brazil

Abstract

Metacaspases are lower eukaryotic peptidases similar to caspases, which are enzymes that participate in the mammalian cell death system. Several types of metacaspases were found in plants, fungi, and protozoa. Cell viability experiments have demonstrated that they, as well as caspases in mammals, are closely correlated with programmed cell death in these organisms. From the standpoint of substrate specificity caspases have an affinity for aspartic acid residues at the P1 position, in addition to important interactions with the specific residues depending on the caspase at positions P2, P3, and P4, so that there are available substrates that are capable of differentiating the various caspases. However, metacaspases have specificity for arginine or lysine residues at the P1 position and to date, there are few studies on the substrate specificity of these enzymes. The present research project has the purpose of cloning the Saccharomyces cerevisiae YCA1 metacarboxase containing the N-terminal amino acid deletion of 86 amino acids, allowing the biochemical characterization of this peptidase.