Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871173 | FEBS Letters | 2013 | 7 Pages |
Abstract
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 α-helix (DJ-1ÎH9) was stronger than that of full-sized DJ-1, and the most susceptible sequence digested by DJ-1ÎH9 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-1ÎH9.
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Authors
Hitomi Mitsugi, Takeshi Niki, Kazuko Takahashi-Niki, Kyoko Tanimura, Kumiko Yoshizawa-Kumagaye, Masahiko Tsunemi, Sanae M.M. Iguchi-Ariga, Hiroyoshi Ariga,