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Molecular Biology Commons

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Microbiology

Theses/Dissertations

2005

Omi/HtrA2

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Full-Text Articles in Molecular Biology

Novel Protein-Protein Interactions Regulate The Proteolytic Activity Of The Pro- Apoptotic Serine Protease, Omi/Htra2, Supriya Singh Jan 2005

Novel Protein-Protein Interactions Regulate The Proteolytic Activity Of The Pro- Apoptotic Serine Protease, Omi/Htra2, Supriya Singh

Electronic Theses and Dissertations

Omi/HtrA2 is a mitochondrial serine protease with high homology to the bacterial HtrA proteins. Omi promotes caspase-dependent apoptosis by binding and degrading IAPs-inhibitor of apoptosis proteins. Omi can also induce caspase-independent apoptosis but the actual mechanism is still unknown. IAP's are not the only substrates cleaved by Omi. There are at least two more known substrates of Omi, the HAX-1 and the ped/pea-15 proteins. HS1-associated protein X-1 (HAX-1) is a mitochondrial protein, degraded by Omi after induction of caspase-dependent apoptosis. Ped/pea-15 is also an anti-apoptotic protein and is cleaved by Omi after induction of caspase-independent apoptosis. The proteolytic activity of …