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Nat Chem Biol. 2017 Aug;13(8):842-844. doi: 10.1038/nchembio.2406. Epub 2017 Jun 12.

Site-specific incorporation of phosphotyrosine using an expanded genetic code.

Author information

1
Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
2
Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, California, USA.
3
Institute for Bioscience and Biotechnology Research, University of Maryland College Park, Rockville, Maryland, USA.
4
The Salk Institute for Biological Studies, Molecular and Cell Biology Laboratory, La Jolla, California, USA.

Abstract

Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is key to understanding the role of protein phosphorylation. Here we report an efficient method to generate pure, active phosphotyrosine-containing proteins by genetically encoding a stable phosphotyrosine analog that is convertible to native phosphotyrosine. We demonstrate its general compatibility with proteins of various sizes, phosphotyrosine sites and functions, and reveal a possible role of tyrosine phosphorylation in negative regulation of ubiquitination.

PMID:
28604697
PMCID:
PMC5577362
DOI:
10.1038/nchembio.2406
[Indexed for MEDLINE]
Free PMC Article

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