RS/tRNA Foundational Publication Support
Bryson, David I., Chenguang Fan, Li-Tao Guo, Corwin Miller, Dieter Söll, and David R. Liu. (dec) 2017. “Continuous Directed Evolution Of Aminoacyl-Trna Synthetases”. Nature Chemical Biology 13: 1253-1260. doi:10.1038/nchembio.2474.
RS/tRNA Pair Development Year
2018
ncAA(s) Incorporated
Pyrrolysine (Pyl)
ncAA Structure (png, jpg, jpeg)
ncAA Utility
serves as a key component in "genetic code expansion" techniques
Nε-(tert-Butoxycarbonyl)-L-lysine (BocLys)
ncAA Structure (png, jpg, jpeg)
ncAA Utility
Extra-‐chromosomal array (low stability), biolistic bombardment. Scattered in different places in animal.
RS Organism of Origin
Parent RS
RS Mutations
V31I
T56P
H62Y
A100E
T56P
H62Y
A100E
tRNA Organism of Origin
Parent tRNA
tRNA Anticodon
CUA
RS/tRNA Availability
Can be purchased from AddGene Plasmid #104073
Used in what cell line?
RS/tRNA Additional Notes
When tested in BL21(DE3) with sfGFP, It exhibited significantly enhanced activity for the incorporation of the non-canonical amino acid BocK. Compared to the wild-type enzyme, it also supports higher levels of reporter gene expression, reflecting improved efficiency in amber suppression. This enhancement is observed consistently across different reporter systems and target positions for BocK incorporation. The mutations responsible for this improvement are located in the N-terminal tRNA-binding domain rather than the active site, suggesting that increased catalytic performance arises from improved tRNA interactions.