The fluorescent proteins revolutionized our ability to study protein function directly in the cell by enabling individual proteins to be selectively labeled through genetic encoding of a fluorescent tag.  As researchers seek to make increasingly sophisticated dynamic measurements of protein function in the cell to unravel molecular mechanism, we designed a chemical tag to combine the advantages of genetic encoding with a modular organic fluorophore.  With TMP-tag, the protein of interest is tagged with E. coli dihydrofolate reductase, which can subsequently be labeled with a cell permeable trimethoprim-fluorophore conjugate.  Here we demonstrate that TMP-tag is a robust cellular reagent.  We present recent results exploiting the modular nature of the chemical tag to generate TMP-tags for specific applications in single-molecule and super-resolution imaging.

TMP-Tag: A chemical surrogate to the fluorescent proteins for live cell imaging

244th National Meeting (2012)

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