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KONG Ying, YE Hui, SHAO Chang, HAO Haiping. Applications of genetic code expansion in the study of lysine acylation[J]. Journal of China Pharmaceutical University, 2023, 54(5): 519-526. DOI: 10.11665/j.issn.1000-5048.2023041401
Citation: KONG Ying, YE Hui, SHAO Chang, HAO Haiping. Applications of genetic code expansion in the study of lysine acylation[J]. Journal of China Pharmaceutical University, 2023, 54(5): 519-526. DOI: 10.11665/j.issn.1000-5048.2023041401
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Applications of genetic code expansion in the study of lysine acylation

  • 1.

    Key Laboratory of Drug Metabolism and Pharmacokinetics, China Pharmaceutical University, Nanjing 210009

  • 2.

    Department of Pharmacy, Shenzhen Luohu People's Hospital, Shenzhen 518005, China

Funds: This study was supported by the National Key Research and Development Program of China (No.2021YFA1301300); the National Natural Science Foundation of China (No.82173783); the Natural Science Foundation of Jiangsu Province (No.BK20220088); the China Postdoctoral Science Foundation (No.2020M681785) and the Guangdong Basic and Applied Basic Research Foundation（No.2021A1515111100）
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  • Received Date: April 13, 2023
  • Revised Date: October 17, 2023
    Graphical Abstract
    • Abstract
  • Lysine acylation is a ubiquitous protein modification that controls various aspects of protein function. However, it can be challenging to decipher the biological function of site-specific acylation modifications in living cells.The recently developed genetic code expansion (GCE) technology has enabled site-specific incorporation of unnatural amino acids (UAAs) that are structurally consistent with the natural acylation modifications in vivo through orthogonal aminoacyl-tRNA synthetase/tRNA pairs, thus facilitating the study of physicochemical properties and biological behaviors of homogeneously acylated proteins.Besides, GCE technology allows for the targeted introduction of UAAs that mimic acylation modifications but cannot be recognized by deacylases, which improves the stability of lysine acylation modification products.Moreover, the insertion of photo-crosslinked UAAs at specific sites of the target protein has been used to elucidate the reciprocal proteome of acylated modified proteins.Based on the introduction of different structural and functional acylation modifications, we described the novel design of GCE technology combined with three types of UAAs, and their application in studying the functional effects of protein acylation modifications on the enzyme activity, protein stability, cellular localization, protein-DNA interactions and protein-protein interactions of target proteins, with a description of the limitations and prospects of GCE technology in studying protein acylation modification.
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    • References (42)
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