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Identification of the recognition sequence and target proteins for DJ-1 protease
Title: | Identification of the recognition sequence and target proteins for DJ-1 protease |
Authors: | Mitsugi, Hitomi Browse this author | Niki, Takeshi Browse this author →KAKEN DB | Takahashi-Niki, Kazuko Browse this author →KAKEN DB | Tanimura, Kyoko Browse this author | Yoshizawa-Kumagaye, Kumiko Browse this author | Tsunemi, Masahiko Browse this author | Iguchi-Ariga, Sanae M. M. Browse this author →KAKEN DB | Ariga, Hiroyoshi Browse this author →KAKEN DB |
Keywords: | DJ-1 | Protease | Biochemistry |
Issue Date: | 19-Aug-2013 |
Publisher: | Elsevier science bv |
Journal Title: | Febs letters |
Volume: | 587 |
Issue: | 16 |
Start Page: | 2493 |
End Page: | 2499 |
Publisher DOI: | 10.1016/j.febslet.2013.06.032 |
PMID: | 23831022 |
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 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. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/53264 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 有賀 寛芳
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