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Title
  • Identification of the recognition sequence and target proteins for DJ-1 protease
Creator

Mitsugi, Hitomi

Niki, Takeshi

Takahashi-Niki, Kazuko

Tanimura, Kyoko

Yoshizawa-Kumagaye, Kumiko

Tsunemi, Masahiko

Iguchi-Ariga, Sanae M. M.

Ariga, Hiroyoshi

Subject
  • Other DJ-1
  • Other Protease
  • Other Biochemistry
  • NDC 464
Description
Other
  • 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.
PublisherElsevier science bv
Date Issued 2013-08-19
Languageeng
NIItypejournal article
VersiontypeAM
Identifier URI http://hdl.handle.net/2115/53264
Relation
  • isIdenticalTo PMID 23831022
  • isIdenticalTo DOI https://doi.org/10.1016/j.febslet.2013.06.032
Journal
    • ISSN 0014-5793
    • Febs letters
    587(16), 2493-2499
File
Oaidate2019-03-15T05:20:38Z