Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system
Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system
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DOI：
10.1016/j.bbrc.2004.06.095
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发表时间：
2004-08-06
影响因子：
3.1
通讯作者：
Ueda, T
中科院分区：
文献类型：
--
作者：
Ying, BW;Taguchi, H;Ueda, T
一个基于最小组纯化组分的蛋白质合成系统被用来研究分子伴侣在新合成多肽折叠中的作用。在我们确定该系统缺乏内在分子伴侣后，直接评价了以共翻译或翻译后方式添加分子伴侣的效果。使用易于聚集的单链抗体作为模型新生链。在翻译过程中触发因子或DnaK系统的参与有效地增加了所产生的功能蛋白的水平。此外，这两个系统也作为伴侣后，翻译已经停止。相比之下，GroEL/ES系统在折叠中显示很少或没有共翻译或翻译后辅助。(C)2004年由Elsevier Inc.出版
A protein-synthesizing system based on a minimal set of purified components was used to investigate the roles molecular chaperones play in the folding of newly synthesized polypeptides. After we ascertained that this system lacks intrinsic chaperones, the effect of adding chaperones in a co-translational or post-translational manner was directly evaluated. An aggregation-prone single-chain antibody was used as the model nascent chain. The participation of the trigger factor or the DnaK system during translation efficiently increased the level of functional protein that was generated. In addition, both systems also acted as chaperones after translation had been stopped. In contrast, the GroEL/ES system showed little or no co- or post-translational assistance in folding. (C) 2004 Published by Elsevier Inc.