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• W3156623977 abstract "Abstract The ability to site-specifically modify proteins at multiple sites in vivo will enable the study of protein function in its native environment with unprecedented levels of detail. Here, we present a versatile two-step strategy to meet this goal involving site-specific encoding of two distinct noncanonical amino acids bearing bioorthogonal handles into proteins in vivo followed by mutually orthogonal labeling. This general approach, that we call d ual e ncoding a nd labeling (DEAL), allowed us to efficiently encoded tetrazine- and azide-bearing amino acids into a protein and demonstrate for the first time that the bioorthogonal labeling reactions with strained alkene and alkyne labels can function simultaneously and intracellularly with high yields when site-specifically encoded in a single protein. Using our DEAL system, we were able to perform topologically-defined protein-protein crosslinking, intramolecular stapling, and site-specific installation of fluorophores all inside living Escherichia coli cells, as well as study the DNA-binding properties of yeast Replication Protein A in vitro . By enabling the efficient dual modification of proteins in vivo , this DEAL approach provides a tool for the characterization and engineering of proteins in vivo ." @default.
• W3156623977 created "2021-04-26" @default.
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• W3156623977 date "2021-04-12" @default.
• W3156623977 modified "2023-10-12" @default.
• W3156623977 title "Genetic Incorporation of Two Mutually Orthogonal Bioorthogonal Amino Acids That Enable Efficient Protein Dual-Labeling in Cells" @default.
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• W3156623977 doi "https://doi.org/10.1101/2021.04.12.439361" @default.
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