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Caged phosphoproteins.

Deborah M Rothman·E James Petersson·M Eugenio Vázquez·Gabriel S Brandt·Dennis A Dougherty·Barbara Imperiali
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Abstract

We present the chemical and biological synthesis of caged phosphoproteins using the in vitro nonsense codon suppression methodology. Specifically, phosphoamino acid analogues of serine, threonine, and tyrosine with a single photocleavable o-nitrophenylethyl caging group were synthesized as the amino acyl tRNA adducts for insertion into full-length proteins. For this purpose, a novel phosphitylating agent was developed. The successful incorporation of these bulky and charged amino acids into the alpha-subunit of the nicotinic acetyl choline receptor (nAChR) and the vasodilator-stimulated phosphoprotein (VASP) using an in vitro translation system is reported.

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Cyclic AMP-Dependent Protein KinasesPhosphoproteinsRNA, Transfer, Amino Acid-SpecificSerineThreonineJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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Deborah M Rothman, E James Petersson, M Eugenio Vázquez, Gabriel S Brandt, Dennis A Dougherty, Barbara Imperiali. 2005-01-26. Caged phosphoproteins.. https://doi.org/10.1021/ja043875c

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