Identification of the recognition sequence and target proteins for DJ-1 protease
Identification of the recognition sequence and target proteins for DJ-1 protease
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DOI：
10.1016/j.febslet.2013.06.032
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发表时间：
2013-08-19
期刊：
影响因子：
3.5
通讯作者：
Ariga, Hiroyoshi
中科院分区：
文献类型：
--
作者：
Mitsugi, Hitomi;Niki, Takeshi;Ariga, Hiroyoshi
DJ-1是家族性帕金森病基因的产物，也是一种癌基因，是一种半胱氨酸蛋白酶，在抗氧化应激反应中发挥作用。本研究利用重组DJ-1和肽库技术，鉴定了DJ-1蛋白酶的识别序列。缺失C-末端α-螺旋的DJ-1（DJ-1 Delta H9）的蛋白酶活性比完整DJ-1的蛋白酶活性更强，并且在pH 5.5和0 mM NaCl的最适条件下，DJ-1 Delta H9最易消化的序列是缬氨酸-赖氨酸-缬氨酸-丙氨酸（VKVA）。二价离子对DJ-1的蛋白酶活性有抑制作用，尤其是Cu ~（2+）。用DJ-1 Delta H9消化含有VKVA的c-abl癌基因1产物（ABL 1）和驱动蛋白家族成员1B（KIF 1B）。蛋白质相互作用的结构化总结：DJ-1通过酶促研究切割IUF 1B（View interaction）DJ-1通过酶促研究切割ABLI（View interaction）（C）2013欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
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.