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Recent Development of Genetic Code Expansion for Posttranslational Modification Studies

期刊

MOLECULES
卷 23, 期 7, 页码 -

出版社

MDPI
DOI: 10.3390/molecules23071662

关键词

genetic code expansion; noncanonical amino acid; unnatural amino acid; posttranslational modification; protein acetylation; protein phosphorylation; protein methylation; protein oxidation

资金

  1. Ralph E. Powe Junior Faculty Enhancement Awards from Oak Ridge Associated Universities
  2. Arkansas Biosciences Institute
  3. University of Arkansas

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Nowadays advanced mass spectrometry techniques make the identification of protein posttranslational modifications (PTMs) much easier than ever before. A series of proteomic studies have demonstrated that large numbers of proteins in cells are modified by phosphorylation, acetylation and many other types of PTMs. However, only limited studies have been performed to validate or characterize those identified modification targets, mostly because PTMs are very dynamic, undergoing large changes in different growth stages or conditions. To overcome this issue, the genetic code expansion strategy has been introduced into PTM studies to genetically incorporate modified amino acids directly into desired positions of target proteins. Without using modifying enzymes, the genetic code expansion strategy could generate homogeneously modified proteins, thus providing powerful tools for PTM studies. In this review, we summarized recent development of genetic code expansion in PTM studies for research groups in this field.

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