Document Detail

Specific protein interaction of human Pag with Omi/HtrA2 and the activation of the protease activity of Omi/HtrA2.
MedLine Citation:
PMID:  16413409     Owner:  NLM     Status:  MEDLINE    
The human PAG gene product (hPag), one member of the TSA/AhpC family, is overexpressed by oxidative stress, which causes apoptosis. To investigate the apoptotic signal transduction mediated by hPag, hPag-binding protein was screened using the yeast two-hybrid system. Omi/HtrA2 was identified as the hPag-binding protein. Omi/HtrA2, a potent proapoptotic factor, is released from the mitochondria into the cytoplasm as the mature form showing serine protease activity during apoptosis in response to oxidative stress. We found that hPag was able to interact with the mature form of Omi/HtrA2, not with the precursor form of Omi/HtrA2. The binding of Omi/HtrA2 to hPag was shown to involve the PDZ-binding domain in Omi/HtrA2. Also, the carboxyl-terminal domain of hPag was shown to be critical for the protein interaction. Using the yeast two-hybrid system and in vitro binding assay, the reduced form of hPag was able to interact with Omi/HtrA2. Interestingly, the protease activity given by the mature form of Omi/HtrA2 was significantly activated by the binding to hPag. Taken together, these results suggest that the specific protein interaction may participate as a molecular switch in modulating cell death in response to oxidative stress.
Seung-Keun Hong; Mee-Kyung Cha; Il-Han Kim
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-10-12
Journal Detail:
Title:  Free radical biology & medicine     Volume:  40     ISSN:  0891-5849     ISO Abbreviation:  Free Radic. Biol. Med.     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-17     Completed Date:  2006-04-13     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8709159     Medline TA:  Free Radic Biol Med     Country:  United States    
Other Details:
Languages:  eng     Pagination:  275-84     Citation Subset:  IM    
Department of Biochemistry, Paichai University, 439-6 Doma-2-Dong Seo-Gu, Taejon 302-735, Korea.
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MeSH Terms
Adaptor Proteins, Signal Transducing
Enzyme Activation / physiology
Membrane Proteins / genetics,  metabolism*
Mitochondrial Proteins
Oxidative Stress / physiology
Peptide Hydrolases / metabolism*
Peroxidase / metabolism
Phosphoproteins / genetics,  metabolism*
Protein Binding / physiology
Recombinant Fusion Proteins / genetics,  metabolism
Serine Endopeptidases / metabolism*
Signal Transduction / physiology
Two-Hybrid System Techniques
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/PAG1 protein, human; 0/Phosphoproteins; 0/Recombinant Fusion Proteins; EC; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.-/Omi serine protease; EC 3.4.21.-/Serine Endopeptidases

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