Site-specific incorporation of ε-N-crotonyllysine into histones.
A novel post-translationally modified amino acid, crotonyllysine (Kcr), was genetically incorporated into proteins in bacterial and mammalian cells using an evolved pyrrolysyl-tRNA/synthetase-tRNA pair. The ability to produce histones with homogenous, site-specific Kcr modifications will be valuable in elucidating the biological role of this recently identified post-translational modification.
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Chan Hyuk
CH
Kim
Mingchao
M
Kang
Hak Joong
HJ
Kim
Abhishek
A
Chatterjee
Peter G
PG
Schultz
D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D006657:Histones; D011994:Recombinant Proteins; C576157:epsilon-N-crotonyllysine; D000604:Amino Acyl-tRNA Synthetases; D008239:Lysine