Reduction of misacylation to the amber suppressor tRNA during site-specific incorporation of unnatural amino acids
スポンサーリンク
概要
- 論文の詳細を見る
Incorporations of unnatural amino acids in proteins are a useful technique in medical and industrial fields. For practical usages, misacylation caused by engineered aminoacyl-tRNA synthetases can be one of the issues lowering the purity of the generated proteins. Since acceptor stems of tRNAs are known to possess identity elements specific for each amino acid, the misacylation is probably caused by non-specificity of the acceptor stems in tRNAs. In this paper, we modified an acceptor stem of tRNATyr, and tested aminoacylation of over 100 modified tRNAs. Finally, we found the acceptor stem sequence for the tRNA with less misacylation for both tyrosine and tyrosine derivative unnatural amino acids.
著者
-
FUJII Akihiko
Institute of Industrial Science, The University of Tokyo
-
ONODERA Kenji
Institute of Industrial Science, The University of Tokyo
-
KAMIJO Shunsuke
Institute of Industrial Science, The University of Tokyo
-
Fujii Akihiko
Institute For Nuclear Study University Of Tokyo : Department Of Physics School Of Science And Techno
-
Onodera Kenji
The University Of Tokyo Institute Of Industrial Science
-
Kamijo Shunsuke
Institute Of Industrial Science The University Of Tokyo
-
Onodera Kenji
Institute Of Industrial Science The University Of Tokyo
関連論文
- Reduction of misacylation to the amber suppressor tRNA during site-specific incorporation of unnatural amino acids
- Analyses of Conditions for KMSSS Loop in Tyrosyl-tRNA Synthetase by Building a Mutant Library
- Selection of Peptide Inhibitors of Soluble Aβ1-42 Oligomer Formation by Phage Display
- Analyses of Conditions for KMSSS Loop in Tyrosyl-tRNA Synthetase by Building a Mutant Library
- Application of the Extended Siegert Theorem to Muon Capture Reactions
- Selection of Peptide Inhibitors of Soluble Aβ_ Oligomer Formation by Phage Display
- Identification of Novel Short Peptide Inhibitors of Soluble 37/48 kDa Oligomers of Amyloid β42
- Muon Capture in He^3
- Identification of Novel Short Peptide Inhibitors of Soluble 37/48kDa Oligomers of Amyloid β42
- Precise Segmentation and Estimation of Pedestrian Trajectory Using On-Board Monocular Cameras
- Inhibition of Aggregation of Amyloid β42 by Arginine-Containing Small Compounds