title: The analysis of histone modifications.
abstract: The biological function of many proteins is often regulated through posttranslational modifications (PTMs). Frequently different modifications influence each other and lead to an intricate network of interdependent modification patterns that affect protein-protein interactions, enzymatic activities and sub-cellular localizations. One of the best-studied class of proteins that is affected by PTMs and combinations thereof are the histone molecules. Histones are very abundant, small basic proteins that package DNA in the eukaryotic nucleus to form chromatin. The four core-histones are densely modified within their first 20-40 N-terminal amino acids, which are highly evolutionary conserved despite playing no structural role. The modifications are thought to constitute a histone code that is used by the cell to encrypt various chromatin conformations and gene expression states. The analysis of modified histones can be used as a model to dissect complex modification patterns and to investigate their molecular functions. Here we review techniques that have been used to decipher complex histone modification patterns and discuss the implication of these findings for chromatin structure and function.
authors.affiliation: Histone modifications group, Adolf-Butenandt Institute, Ludwig-Maximilians University of Munich, Schillerstr 44, 80336 Munich, Germany.
authors.forename: Ana
authors.initials: A
authors.lastname: Villar-Garea
authors.forename: Axel
authors.initials: A
authors.lastname: Imhof
mesh_terms: D000595:Amino Acid Sequence; D000917:Antibody Formation; D006657:Histones / Q000276:immunology / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones; D008239:Lysine