Journal
SCIENCE
Volume 333, Issue 6046, Pages 1151-1154Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1207203
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Funding
- NSF [MCB-0645283, MCB-0950474]
- National Institute of General Medical Sciences [GM 22854]
- National Research Foundation of Korea [ABC-20100029737]
- National Institute of Diabetes and Digestive and Kidney Diseases [K01DK089006]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0950474] Funding Source: National Science Foundation
- National Research Foundation of Korea [2011-0031357] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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O-Phosphoserine (Sep), the most abundant phosphoamino acid in the eukaryotic phosphoproteome, is not encoded in the genetic code, but synthesized posttranslationally. Here, we present an engineered system for specific cotranslational Sep incorporation (directed by UAG) into any desired position in a protein by an Escherichia coli strain that harbors a Sep-accepting transfer RNA (tRNA(Sep)), its cognate Sep-tRNA synthetase (SepRS), and an engineered EF-Tu (EF-Sep). Expanding the genetic code rested on reengineering EF-Tu to relax its quality-control function and permit Sep-tRNA(Sep) binding. To test our system, we synthesized the activated form of human mitogen-activated ERK activating kinase 1 (MEK1) with either one or two Sep residues cotranslationally inserted in their canonical positions (Sep(218), Sep(222)). This system has general utility in protein engineering, molecular biology, and disease research.
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