Title

Determining The Role Of Mtm1 In Glutathione Metabolism

Author(s)

Kaileigh Collins

School Name

Governor's School for Science and Math

Grade Level

12th Grade

Presentation Topic

Biochemistry

Presentation Type

Mentored

Mentor

Mentor: Dr. Outten; Department of Chemistry and Biochemistry, University of South Carolina

Abstract

Mitochondria are compartmentalized into the outer and inner membranes, the intermediate space (IMS), and the matrix. It contains specific sets of proteins and mitochondrial DNA. Most of the mitochondrial proteins are synthesized as precursors in the cytoplasm and transported across the mitochondrial membranes. As the major site of cellular respiration, mitochondrion is subjected to harmful reactive oxygen species that are combatted by cellular antioxidant mechanisms comprising of Superoxide Dimutase 2 (SOD2) and Glutathione (GSH). Mtm1 is a metal carrier protein in model eukaryote S. Cerevisae that is reported to activate mitochondrial SOD2. The mitochondrial glutathione pool comprises 10-15% of the cellular glutathione and is derived from the transport of cytosolic glutathione across the mitochondrial membranes. While there are many studies of SOD2, not much is known about GSH and its transport into the mitochondria. Since Mtm1 is found to be involved in mitochondrial redox homeostasis, it is suspected to have a role in Glutathione metabolism. In a Wild Type BY4741 S. Cerevisae yeast strain, Mtm1 was deleted through Lithium Acetate transformation. Transformed and control strains were grown and a mitochondrial isolation was performed. The levels of GSH were analyzed through a Glutathione assay. When Mtm1 was deleted, Glutathione complies in the Post-Mitochondrial Supernatant (PMS). There was a decrease in levels of GSH in the mitochondria when comparing the transformed strain to the BY4741 strain. In short, Mtm1 is a carrier protein for Glutathione. In the future, Glutathione Disulfide (GSSG) will be tested for because it reduces the loss of GSH.

Location

Owens 203

Start Date

4-16-2016 9:30 AM

COinS
 
Apr 16th, 9:30 AM

Determining The Role Of Mtm1 In Glutathione Metabolism

Owens 203

Mitochondria are compartmentalized into the outer and inner membranes, the intermediate space (IMS), and the matrix. It contains specific sets of proteins and mitochondrial DNA. Most of the mitochondrial proteins are synthesized as precursors in the cytoplasm and transported across the mitochondrial membranes. As the major site of cellular respiration, mitochondrion is subjected to harmful reactive oxygen species that are combatted by cellular antioxidant mechanisms comprising of Superoxide Dimutase 2 (SOD2) and Glutathione (GSH). Mtm1 is a metal carrier protein in model eukaryote S. Cerevisae that is reported to activate mitochondrial SOD2. The mitochondrial glutathione pool comprises 10-15% of the cellular glutathione and is derived from the transport of cytosolic glutathione across the mitochondrial membranes. While there are many studies of SOD2, not much is known about GSH and its transport into the mitochondria. Since Mtm1 is found to be involved in mitochondrial redox homeostasis, it is suspected to have a role in Glutathione metabolism. In a Wild Type BY4741 S. Cerevisae yeast strain, Mtm1 was deleted through Lithium Acetate transformation. Transformed and control strains were grown and a mitochondrial isolation was performed. The levels of GSH were analyzed through a Glutathione assay. When Mtm1 was deleted, Glutathione complies in the Post-Mitochondrial Supernatant (PMS). There was a decrease in levels of GSH in the mitochondria when comparing the transformed strain to the BY4741 strain. In short, Mtm1 is a carrier protein for Glutathione. In the future, Glutathione Disulfide (GSSG) will be tested for because it reduces the loss of GSH.