Co-translational Installation of Posttranslational Modifications by Non-canonical Amino Acid Mutagenesis

被引：7

作者：

Niu, Wei ^{[1
,3
]}

Guo, Jiantao ^{[2
,3
]}

机构：

[1] Univ Nebraska Lincoln, Dept Chem & Biomol Engn, Lincoln, NE 68588 USA

[2] Univ Nebraska Lincoln, Dept Chem, Lincoln, NE 68588 USA

[3] Univ Nebraska Lincoln, Nebraska Ctr Integrated Biomol Commun NCIBC, Lincoln, NE 68588 USA

来源：

CHEMBIOCHEM | 2023年

关键词：

co-translational modification; genetic code expansion; noncanonical amino acid; protein posttranslational modification; PTM analogs; SITE-SPECIFIC INCORPORATION; TYROSINE-SULFATED PROTEINS; TRANSFER-RNA SYNTHETASE; L-THREONINE KINASE; GENETIC-CODE; ESCHERICHIA-COLI; LYSINE ACETYLATION; THIOACETYL-LYSINE; CHEMICAL BIOLOGY; SELECTIVE INCORPORATION;

D O I：

10.1002/cbic.202300039

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein posttranslational modifications (PTMs) play critical roles in regulating cellular activities. Here we provide a survey of genetic code expansion (GCE) methods that were applied in the co-translational installation and studies of PTMs through noncanonical amino acid (ncAA) mutagenesis. We begin by reviewing types of PTM that have been installed by GCE with a focus on modifications of tyrosine, serine, threonine, lysine, and arginine residues. We also discuss examples of applying these methods in biological studies. Finally, we end the piece with a short discussion on the challenges and the opportunities of the field.

引用

页数：10

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