期刊
NATURE COMMUNICATIONS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms9130
关键词
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资金
- National Institutes of Health [NIDDK-K01DK089006, P01DK01743341, NIH-MSTP-TG-T32GM07205]
- Defense Advanced Research Projects Agency [N66001-12-C-4211]
- DuPont, Inc.
- Gen9, Inc.
- Arnold and Mabel Beckman Foundation
- National Science Foundation Graduate Research Fellowship [DGE-1122492]
- [NIH-T32GM100884]
Biochemical investigation of protein phosphorylation events is limited by inefficient production of the phosphorylated and non-phosphorylated forms of full-length proteins. Here using a genomically recoded strain of E. coli with a flexible UAG codon we produce site-specific serine-or phosphoserine-containing proteins, with purities approaching 90%, from a single recombinant DNA. Specifically, we synthesize human MEK1 kinase with two serines or two phosphoserines, from one DNA template, and demonstrate programmable kinase activity. Programmable protein phosphorylation is poised to help reveal the structural and functional information encoded in the phosphoproteome.
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