Back

Title	en Identification of the recognition sequence and target proteins for DJ-1 protease
Creator	en Mitsugi, Hitomi en Niki, Takeshi NRID 1000090377193 en Takahashi-Niki, Kazuko NRID 1000050447645 en Tanimura, Kyoko en Yoshizawa-Kumagaye, Kumiko en Tsunemi, Masahiko en Iguchi-Ariga, Sanae M. M. NRID 1000090184283 en Ariga, Hiroyoshi NRID 1000020143505
Accessrights	open access
Subject	Other en DJ-1 Other en Protease Other en Biochemistry NDC 464
Description	Abstract en 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.
Publisher	en Elsevier science bv
Date	Issued2013-08-19
Language	eng
Resource Type	journal article
Version Type	AM
Identifier	HDL http://hdl.handle.net/2115/53264
Relation	isVersionOf DOI https://doi.org/10.1016/j.febslet.2013.06.032 PMID 23831022
Journal	PISSN 0014-5793 en Febs letters Volume Number587 Issue Number16 Page Start2493 Page End2499
File	fulltext Mitsugi et al..pdf 2.66 MB (application/pdf) Issued2013-08-19
Oaidate	2023-07-26