title: Quantification of histone modifications using ¹⁵N metabolic labeling.
abstract: Mass spectrometry has made major contributions to recent discoveries in the field of epigenetics, particularly in the characterization of the myriad post-translational modifications (PTMs) of histones which are technically challenging to analyze. These new developments have further aroused great interest in development of robust, new mass spectrometric methods to quantitatively study the dynamics of histone modifications. This review covers quantitative analysis of histone PTMs and discuss an ¹⁵N metabolic labeling procedure for quantifying histone PTMs applied to the analysis of methyltransferase knockouts in the model organism, Tetrahymena thermophila.
authors: Department of Computational Medicine and Bioinformatics, University of Michigan, USA.
authors: Chunchao
authors: C
authors: Zhang
authors: Yifan
authors: Y
authors: Liu
authors: Philip C
authors: PC
authors: Andrews
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006657:Histones / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007553:Isotope Labeling; D013058:Mass Spectrometry; D008745:Methylation; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016808:Tetrahymena thermophila / Q000235:genetics / Q000378:metabolism*
chemical_list: D006657:Histones; D009587:Nitrogen Isotopes; D010455:Peptides; D011994:Recombinant Proteins