Identification of the recognition sequence and target proteins for DJ-1 protease
Iguchi-Ariga, Sanae M. M.
DJ-1, the product of familial Parkinson's disease gene and an oncogene, is a cysteine protease which plays a role in anti-oxidative stress reaction. In this study, we identified the recognition sequence for DJ-1 protease by using recombinant DJ-1 and a peptide library. Protease activity of DJ-1 lacking C-terminal alpha-helix (DJ-1 Delta H9) was stronger than that of full-sized DJ-1, and the most susceptible sequence digested by DJ-1 Delta H9 was valine-lysine-valine-alanine (VKVA) under the optimal conditions of pH 5.5 and 0 mM NaCl. Divalent ions, especially Cu2+, were inhibitory to DJ-1's protease activity. c-abl oncogene 1 product (ABL1) and kinesin family member 1B (KIF1B) containing VKVA were digested by DJ-1 Delta H9. Structured summary of protein interactions: DJ-1 cleaves IUF1B by enzymatic study (View interaction) DJ-1 cleaves ABLI by enzymatic study (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
|Publisher||Elsevier science bv
|Date|| Issued 2013-08-19
|Identifier|| URI http://hdl.handle.net/2115/53264