期刊
ACS SYNTHETIC BIOLOGY
卷 7, 期 2, 页码 689-695出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssynbio.7b00408
关键词
genetic code expansion; post-translational modification; phosphorylation; acetylation; noncanonical amino acid
资金
- National Institutes of Health (National Institute of Allergy and Infectious Diseases) [AI119813]
- University of Arkansas
- Arkansas Biosciences Institute
Post-translational modifications (PTMs) play important roles in regulating a variety of biological processes. To facilitate PTM studies, the genetic code expansion strategy has been utilized to cotranslationally incorporate individual PTMs such as acetylation and phosphorylation into proteins at specific sites. However, recent studies have demonstrated that PTMs actually work together to regulate protein functions and structures. Thus, simultaneous incorporation of multiple distinct PTMs into one protein is highly desirable. In this study, we utilized the genetic incorporation systems of phosphoserine and acetyllysine to install both phosphorylation and acetylation into target proteins simultaneously in Escherichia coli. And we used this system to study the effect of coexisting acetylation and phosphorylation on malate dehydrogenase, demonstrating a practical application of this system in biochemical studies. Furthermore, we tested the mutual orthogonality of three widely used genetic incorporation systems, indicating the possibility of incorporating three distinct PTMs into one protein simultaneously.
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