biostudies-literatureXiao HNational Institute of General Medical SciencesNIGMS NIH HHS1599-603https://www.ebi.ac.uk/biostudies/studies/S-EPMC4506705biostudies-literatureUnknown10(7)Here, we report the evolution of an orthogonal amber suppressor pyrrolysyl-tRNA synthetase (PylRS)/tRNACUA(Pyl) pair that genetically encodes the post-translationally modified amino acid, ε-N-2-hydroxyisobutyryl-lysine (HibK), in bacteria and mammalian cells. HibK is a new type of histone mark that is widely distributed in histone proteins. The ability to site-specifically incorporate HibK into proteins provides a useful tool to probe the biological function of this newly identified post-translational modification.ACS chemical biologyGenetic Incorporation of ε-N-2-Hydroxyisobutyryl-lysine into Recombinant Histones.PMC4506705R01 GM097206R01 GM097206-04Xiao HXuan WLiu TSchultz PGShao SfalseGenetic Incorporation of ε-N-2-Hydroxyisobutyryl-lysine into Recombinant Histones.Here, we report the evolution of an orthogonal amber suppressor pyrrolysyl-tRNA synthetase (PylRS)/tRNACUA(Pyl) pair that genetically encodes the post-translationally modified amino acid, ε-N-2-hydroxyisobutyryl-lysine (HibK), in bacteria and mammalian cells. HibK is a new type of histone mark that is widely distributed in histone proteins. The ability to site-specifically incorporate HibK into proteins provides a useful tool to probe the biological function of this newly identified post-translational modification.2015-01-01T00:00:00Z2015 Jul2024-11-20T03:22:18.832Z2019-03-27T01:55:22ZS-EPMC45067052590983410.1021/cb501055h