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Identification of the recognition sequence and target proteins for DJ‐1 protease
Author(s) -
Mitsugi Hitomi,
Niki Takeshi,
Takahashi-Niki Kazuko,
Tanimura Kyoko,
Yoshizawa-Kumagaye Kumiko,
Tsunemi Masahiko,
Iguchi-Ariga Sanae M.M.,
Ariga Hiroyoshi
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.06.032
Subject(s) - protease , valine , biochemistry , peptide sequence , serine protease , recombinant dna , chemistry , biology , microbiology and biotechnology , enzyme , gene , amino acid
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‐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.