The yeast two-hybrid system was used to isolate and characterize protein interactors of the N-terminal domain of the serine protease Omi/HtrA2 (high temperature requirement protein A2) encompassing amino acids 31-133. This large domain of Omi/HtrA2 is usually cleaved and removed through autoproteolysis to produce the mature form of the protein. Whether the N-terminal domain has any function after its removal is unknown. Omi/HtrA2 is involved in a variety of diseases including cancers, neurodegenerative disorders, and metabolic disorders, but thus far, it is assumed that its normal function is the degradation of specific substrates. To characterize any potential function of Omi/HtrA2’s unique amino terminus, specific interactors were isolated. One such interactor was the small GTPase Rab2A protein. We discuss the implications of this interaction and its biological significance.
Zervos, Antonis S.
Bachelor of Science (B.S.)
College of Medicine
Burnett School of Biomedical Sciences
Orlando (Main) Campus
Nguyen, Christine, "Characterizing the Function of the N-Terminal Domain of Omi/HtrA2" (2017). Honors Undergraduate Theses. 242.