Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system

Bei Wen Ying, Hideki Taguchi, Hiroshi Ueda, Takuya Ueda

研究成果: Article査読

39 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1359-1364
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
320
4
DOI
出版ステータスPublished - 2004 8月 6
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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