TePhe, a tellurium-containing phenylalanine mimic, allows monitoring of protein synthesis in vivo with mass cytometry.
Protein synthesis is central to maintaining cellular homeostasis and its study is critical to understanding the function and dysfunction of eukaryotic systems. Here we report L-2-tellurienylalanine (TePhe) as a noncanonical amino acid for direct measurement of protein synthesis. TePhe is synthetically accessible, nontoxic, stable under biological conditions, and the tellurium atom allows its direct detection with mass cytometry, without postexperiment labeling. TePhe labeling is competitive with phenylalanine but not other large and aromatic amino acids, demonstrating its molecular specificity as a phenylalanine mimic; labeling is also abrogated in vitro and in vivo by the protein synthesis inhibitor cycloheximide, validating TePhe as a translation reporter. In vivo, imaging mass cytometry with TePhe visualizes translation dynamics in the mouse gut, brain, and tumor. The strong performance of TePhe as a probe for protein synthesis, coupled with the operational simplicity of its use, suggests TePhe could become a broadly applied molecule for measuring translation in vitro and in vivo.
['Bassan|Jay|J|0000-0003-3682-4629', 'Willis|Lisa M|LM|', 'Vellanki|Ravi N|RN|', 'Nguyen|Alan|A|', 'Edgar|Landon J|LJ|', 'Wouters|Bradly G|BG|', 'Nitz|Mark|M|']
D000596:Amino Acids D000818:Animals D001921:Brain D003513:Cycloheximide D005434:Flow Cytometry D045325:HCT116 Cells D006801:Humans D019044:Image Cytometry D007583:Jejunum D019169:Jurkat Cells D051379:Mice D009374:Neoplasms, Experimental D010649:Phenylalanine D014176:Protein Biosynthesis D011500:Protein Synthesis Inhibitors D013691:Tellurium
protein synthesis mass cytometry tellurium