論文

査読有り
2015年12月

Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system

SCIENTIFIC REPORTS
  • Tatsuya Niwa
  • ,
  • Yoshihiro Sasaki
  • ,
  • Eri Uemura
  • ,
  • Shugo Nakamura
  • ,
  • Minato Akiyama
  • ,
  • Mitsuru Ando
  • ,
  • Shinichi Sawada
  • ,
  • Sada-atu Mukai
  • ,
  • Takuya Ueda
  • ,
  • Hideki Taguchi
  • ,
  • Kazunari Akiyoshi

5
開始ページ
18025
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/srep18025
出版者・発行元
NATURE PUBLISHING GROUP

Membrane proteins play pivotal roles in cellular processes and are key targets for drug discovery. However, the reliable synthesis and folding of membrane proteins are significant problems that need to be addressed owing to their extremely high hydrophobic properties, which promote irreversible aggregation in hydrophilic conditions. Previous reports have suggested that protein aggregation could be prevented by including exogenous liposomes in cell-free translation processes. Systematic studies that identify which membrane proteins can be rescued from irreversible aggregation during translation by liposomes would be valuable in terms of understanding the effects of liposomes and developing applications for membrane protein engineering in the context of pharmaceutical science and nanodevice development. Therefore, we performed a comprehensive study to evaluate the effects of liposomes on 85 aggregation-prone membrane proteins from Escherichia coli by using a reconstituted, chemically defined cell-free translation system. Statistical analyses revealed that the presence of liposomes increased the solubility of > 90% of the studied membrane proteins, and ultimately improved the yields of the synthesized proteins. Bioinformatics analyses revealed significant correlations between the liposome effect and the physicochemical properties of the membrane proteins.

Web of Science ® 被引用回数 : 18

リンク情報
DOI
https://doi.org/10.1038/srep18025
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26667602
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000366390600001&DestApp=WOS_CPL