title: Methods to identify and functionally analyze factors that specifically recognize histone lysine methylation.
abstract: Histone lysine methylation plays an important role in the regulation of gene expression and impacts many fundamental biological processes, such as cellular identity. Despite great efforts, the mechanisms behind the downstream consequences of histone methyl-recognition remain poorly understood. Here, we describe various methods to investigate specific histone lysine-methyl recognition, including the use of short peptides, histone octamers, and the more physiological nucleosomal arrays. We also discuss techniques that are well suited to assess functional aspects of binding as it relates to transcriptional regulation.
authors.affiliation: Division of Nucleic Acids Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School Piscataway, NJ 08854-5635, USA.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Sims
authors.forename: Patrick
authors.initials: P
authors.lastname: Trojer
authors.forename: Guohong
authors.initials: G
authors.lastname: Li
authors.forename: Danny
authors.initials: D
authors.lastname: Reinberg
mesh_terms: D000345:Affinity Labels; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D004268:DNA-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D005786:Gene Expression Regulation / Q000502:physiology; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D011994:Recombinant Proteins; D014158:Transcription, Genetic / Q000502:physiology; D014981:Xenopus
chemical_list: D000345:Affinity Labels; D004268:DNA-Binding Proteins; D006657:Histones; D011994:Recombinant Proteins; D008239:Lysine