RS/tRNA Foundational Publication Support
Zhang, F., Q. Zhou, G. Yang, L. An, F. Li, and J. Wang. n.d. “A Genetically Encoded 19F Nmr Probe For Lysine Acetylation” 54: 3879+.
RS/tRNA Pair Development Year
2018
ncAA(s) Incorporated
N6-Trifluoroacetyl-L-lysine
ncAA Structure (png, jpg, jpeg)
ncAA Utility
They are used for sites specifically studying post-translational modification acetylation events on particular lysine residues. Also be used as an F19 NMR probe.
Nε-acetyl-L-lysine
ncAA Structure (png, jpg, jpeg)
ncAA Utility
They are used for sites specifically studying post-translational modification acetylation events on particular lysine residues.
RS Organism of Origin
Parent RS
RS Mutations
L266M
L270I
L274A
C313F
L270I
L274A
C313F
tRNA Organism of Origin
Parent tRNA
tRNA Anticodon
CUA
Other tRNA Mutations
N/A
Multiple tRNAs?
N/A
RS/tRNA Availability
not commercially available
RS/tRNA Additional Notes
Using 2 mM TFAcK yielded ~ 1 mg/L myoglobin(4), with MS confirming high fidelity incorporation, and showed it was not deacetylated in E. coli. Also produced p53(164) with high fidelity by MS and show it was recognized by an anti Acetyl-Lys antibody and also resistant to hydrolysis by sirtuin 2, while the AcK protein was hydrolyzed. In HEK cells, using 1 mM TFAcK installed into EGFP(37) simply monitoring successful incorporation by ncAA-dependent fluorescence. The RS was also shown to work with AcK, but yields and fidelity were not quantified.