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Novel Protein-protein Interactions Regulate the Proteolytic Activity of the Pro-apoptotic Serine Protease, Omi/HtrA2

Supriya Singh

出版	University of Central Florida, 2005
URL	http://books.google.com.hk/books?id=QPvjzQEACAAJ&hl=&source=gbs_api

註釋

My project was aimed to investigate the normal function of Omi in cell death and the mechanism of its regulation by isolating and characterizing novel Omi interactors. I screened a human melanocyte cDNA library using the yeast-two-hybrid system and Omi as the "bait" protein. Human Rad21 protein was isolated as a specific novel interactor of Omi. Human Rad21 interacted with the PDZ domain of Omi, the part of the protein known to be involved in protein-protein interactions. Human Rad21 is a nuclear protein that plays a role in DNA double-strand break repair and sister chromatid cohesion during metaphase. Several reports suggest hRad21 has also a role in apoptosis; it is cleaved by caspase-3 and part of the protein becomes cytoplasmic. Human Rad21 was not cleaved by Omi in vitro and therefore it is unlikely to be a substrate. When tested in a proteolytic assay Rad21 was able to increase the proteolytic activity of Omi