Protein Binding Partners of Glutathione Transferase Theta 1 (GSTT1)

Abstract

Glutathione transferase (GST) enzymes are found in all kingdoms of life. Their catalytic activity is well characterized: conjugation of glutathione with electrophiles, a process which inactivates many toxic chemicals. Additionally, several GST enzymes participate in cell signaling processes, mediated by protein binding interactions. This thesis focuses on human GST theta 1. 30-40% of the human population is homozygous null for the GSTT1 gene, but the consequences of this polymorphism remain unclear. I have searched for possible protein binding partners of GSTT1 through a pull-down assay with protein lysates from cultured human prostate cancer cells and erythrocytes, followed by mass spectrometry-based proteomic analysis. Histidine Triad Nucleotide Binding Protein-1 (HINT1) was identified as a binding partner. HINT1, a member of the HIT superfamily of nucleotide hydrolases and transferases; is also known to be a tumor suppressor. An interaction between GSTT1 and HINT1 may point towards a previously unknown biological role of GSTT1.

Description

Keywords

Glutathione Transferase, GSTT1, HINT1, protein binding partners

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