Identification of the recognition sequence and target proteins for DJ‐1 protease
2013; Wiley; Volume: 587; Issue: 16 Linguagem: Inglês
10.1016/j.febslet.2013.06.032
ISSN1873-3468
AutoresHitomi Mitsugi, Takeshi Niki, Kazuko Takahashi-Niki, Kyoko Tanimura, Kumiko Yoshizawa‐Kumagaye, Masahiko Tsunemi, Sanae M.M. Iguchi‐Ariga, Hiroyoshi Ariga,
Tópico(s)RNA regulation and disease
ResumoDJ‐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‐1ΔH9) was stronger than that of full‐sized DJ‐1, and the most susceptible sequence digested by DJ‐1ΔH9 was valine–lysine–valine–alanine (VKVA) under the optimal conditions of pH 5.5 and 0 mM NaCl. Divalent ions, especially Cu 2+ , 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‐1ΔH9.
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