Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 58, Issue -, Pages 112-120Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2020.07.012
Keywords
Genetic code expansion; Unnatural amino acids; Proximity-triggered crosslinking; Photocrosslinking; Photocaging; Post-translational modifications
Categories
Funding
- Excellence Initiative CIPSM
- DFG through the SFB1035 program (German Research Foundation DFG) [Sonderforschungsbereich 1035, 201302640]
- Excellence Initiative
- EUMarie Curie COFUND Program
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In recent years it has become possible to genetically encode an expanded set of designer amino acids with tailored chemical and physical properties (dubbed unnatural amino acids, UAAs) into proteins in living cells by expanding the genetic code. Together with developments in chemistries that are amenable to and selective within physiological settings, these strategies have started to have a big impact on biological studies, as they enable exciting in cellulo applications. Here we highlight recent advances to covalently stabilize transient protein-protein interactions and capture enzyme substrate complexes in living cells using proximity-triggered and residue-selective photo-induced crosslinking approaches. Furthermore, we describe recent efforts in controlling enzyme activity with photocaged UAAs and in extending their application to a variety of enzymatic scaffolds. In addition, we discuss the site specific incorporation of UAAs mimicking post-translational modifications (PTMs) and approaches to generate natively-linked ubiquitin-protein conjugates to probe the role of PTMs in modulating complex cellular networks.
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