泛素羧基端水解酶UCH家族水解反应动力学研究
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摘要
在蛋白质的泛素-蛋白酶体降解途径中,蛋白质的泛素化与去泛素化是一个极其复杂而关键的过程。泛素羧基端水解酶可特异性地切除泛素羧基端融合的氨基酸或肽链,无论从结构和功能上讲,都可以说是大量去泛素化酶中极具有代表性的一个家族。为了研究UCH家族在去泛素化反应中是否具有底物特异性的问题,我们将泛素第45位的苯丙氨酸突变为色氨酸(Ub~(F45W)),并在此基础上于原核表达系统中构建一系列在泛素羧基端融合的第一个残基存在差异的肽段(Ub~(F45W)-Xaa-His6 tag)作为酶切反应的底物。在反应中止后用Ni柱亲和层析的方法除去反应体系中带有His6标记的蛋白质,然后通过荧光测定反应产物Ub~(F45W)的浓度,进而定量计算出不同泛素羧基端水解酶的酶解活力。实验结果显示, UCH-L1,UCH37对于X位不同的泛素融合蛋白是具有底物选择性并且彼此间存在差异,而UCH-L3则不具有底物选择性。
Ubiquitin C-terminal hydrolases (UCHs) belong to a representative family of deubiquitinating enzymes (DUBs), which specifically cleave ubiquitin (Ub) chains or extensions. Here we describe a convenient method by the subustrates of Phe45Trp Ub-fusion proteins (Ub~(F45W)-Xaa) for characterizing substrate specificities of various UCHs. After removal of the His6-tagged proteins by Ni-NTA affinity, the enzymatic activities of the UCHs are quantitatively determined by fluorescence assay of the Ub~(F45W) product. The results suggest that three UCHs, UCH-L1, UCH-L3 and UCH37 have discrimination in their substrate specificities for the Ub extension proteins. This method may also be applicable to testing the substrate specificities of other DUBs.
Ubiquitin C-terminal hydrolases (UCHs) belong to a representative family of deubiquitinating enzymes (DUBs), which specifically cleave ubiquitin (Ub) chains or extensions. Here we describe a convenient method by the subustrates of Phe45Trp Ub-fusion proteins (Ub~(F45W)-Xaa) for characterizing substrate specificities of various UCHs. After removal of the His6-tagged proteins by Ni-NTA affinity, the enzymatic activities of the UCHs are quantitatively determined by fluorescence assay of the Ub~(F45W) product. The results suggest that three UCHs, UCH-L1, UCH-L3 and UCH37 have discrimination in their substrate specificities for the Ub extension proteins. This method may also be applicable to testing the substrate specificities of other DUBs.
引文
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[10] Hasegawa K., Funayama M., Matsuura N., Furusawa H., Sakai F., Kowa H., Obata F., Analysis of alpha-synuclein, parkin, tau, and UCH-L1 in a Japanese family with autosomal dominant parkinsonism, Eur Neurol, 2001, 46(1): 20-24
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[12] Elbaz A., Levecque C., Clavel J., S18Y polymorphism in the UCH-L1 gene and Parkinson's disease: evidence for an age-dependent relationship, Mov Disord, 2003, 18(2): 130-137
[13] Carmine B. A., Westerlund M., Bergman O., Nissbrandt H., Lind C., Sydow O., Galter D., S18Y in ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) associated with decreased risk of Parkinson's disease in Sweden. Parkinsonism Relat Disord, 2007,13(5): 295-298
[14] Choi J., Levey A. I., Weintraub S. T., Rees H. D., Gearing M., Chin L. S., Li L., Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases, J Biol Chem, 2004, 279(13): 13256-64
[15] Zhang J., Hattori N., Leroy E., Morris H. R., Kubo S. I., Kobayashi T., Wood N. W., Polymeropoulous M. H., Mizuno Y., Association between a polymorphism of ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) gene and sporadic Parkinson's disease[Parkinsonism Relat Disord 6(4)(2000)195-197], 2002, 9(2): 127
[16] Kwon J.,Kikuchi T., Setsuie R., Ishii Y., Kyuwa S., Yoshikawa Y., Characterization of the testis in congenitally ubiquitin carboxy-terminal hydrolase-1 (Uch-L1) defective (gad) mice, Exp Anim, 2003, 52(1): 1-9
[17] Liu Y., Lashuel H. A., Choi S., Xing X. C., Case A., Ni J., Yeh L. A., Cuny G. D., Stein R. L., Lansbury Jr P. T., Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line, Chem Biol, 2003, 10(9): 837-846
[18] Shi Q., Tao E., An Ile93Met substitution in the UCH-L1 gene is not a disease-causing mutation for idiopathic Parkinson's disease, Chin Med J (Engl), 2003, 116: 312-313
[19] Ardley H. C., Scott G. B., Rose S. A., Tan N. G., Robinson P. A., UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease, J Neurochem, 2004, 90: 379-391
[20] Bonin M., Poths S., Osaka H., Wang Y. L., Wada K., Riess O., Microarray expression analysis of gad mice implicates involvement of Parkinson's disease associated UCH-L1 in multiple metabolic pathways, Brain Res Mol Brain Res, 2004, 126(1): 88-97
[21] Li Z., Melandri F., Berdo I., Jansen M., Hunter L., Wright S., Valbrun D., Figueiredo-Pereira M. E., Delta12-Prostaglandin J2 inhibits the ubiquitin hydrolase UCH-L1 and elicits ubiquitin-protein aggregation without proteasome inhibition, Biochem Biophys Res Commun, 2004, 319(4): 1171-1180
[22] Das C., Hoang Q. Q., Kreinbring C. A., Luchansky S. J., Meray R. K., Ray S. S., Lansbury P. T., Ringe D., Petsko G. A., Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1, Proc Natl Acad Sci U S A, 2006, 103(12): 4675-4680
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