Generation of SUMO-1 modified proteins in E-coli:: towards understanding the biochemistry/structural biology of the SUMO-1 pathway
Generation of SUMO-1 modified proteins in E-coli:: towards understanding the biochemistry/structural biology of the SUMO-1 pathway
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DOI：
10.1016/s0014-5793(04)00321-7
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发表时间：
2004-04-23
期刊：
影响因子：
3.5
通讯作者：
Saitoh, H
中科院分区：
文献类型：
--
作者：
Uchimura, Y;Nakao, M;Saitoh, H
在这里，我们开发了一种二元载体系统，将合成的 SUMO-1 缀合途径引入大肠杆菌，并证明可以有效产生大量的 sumoylated Ran GTPase 激活蛋白 1 C 末端区域 (RanGAP1-C2)、Ran 结合蛋白 2 内部重复结构域、p53 和早幼粒细胞白血病。苏酰化的重组 RanGAP1-C2 似乎保留了体内特性，因为正如体内研究所预期的那样，它在赖氨酸 517 处被特异性苏酰化。我们的研究结果表明建立了一条生产大量苏酰化重组蛋白的生物合成途径，这将为研究 SUMO-1 修饰途径的生化和结构方面开辟新途径。 (C) 2004 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
Here, we developed a binary vector system that introduces a synthetic SUMO-1 conjugation pathway into Escherichia coli and demonstrated that large amounts of sumoylated Ran GTPase activating protein 1 C-terminal region (RanGAP1-C2), Ran binding protein 2 internal repeat domain, p53 and promyelocytic leukemia were efficiently produced. The sumoylated recombinant RanGAP1-C2 appeared to retain the in vivo properties, since it was specifically sumoylated at lysine 517 as expected from in vivo studies. Our findings indicate the establishment of a biosynthetic route for producing large amounts of sumoylated recombinant proteins that will open up new avenues for studying the biochemical and structural aspects of the SUMO-1 modification pathway. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.