title: Synthesis of ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine containing histone H3 using the pyrrolysine system.
abstract: Recently new lysine modifications were detected in histones and other proteins. Using the pyrrolysine amber suppression system we genetically inserted three of the new amino acids ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine site specifically into histone H3. The lysine at position 9 (H3 K9), which is known to be highly modified in chromatin, was replaced by these unnatural amino acids.
authors.affiliation: Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians-Universität, Munich, Butenandtstrasse 5-13, D-81377, Munich, Germany.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Gattner
authors.forename: Milan
authors.initials: M
authors.lastname: Vrabel
authors.forename: Thomas
authors.initials: T
authors.lastname: Carell
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis / Q000737:chemistry; D015153:Blotting, Western; D000440:Butanols / Q000737:chemistry; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular
chemical_list: D000596:Amino Acids; D000440:Butanols; D006657:Histones; C007153:crotonyl alcohol; C456839:pyrrolysine; D008239:Lysine