title: Validation of protein acetylation by mass spectrometry.
abstract: Due to the key role of posttranslational modifications (PTMs) such as lysine acetylation in numerous signaling and regulatory pathways, the ability to identify novel PTMs and to quantify their abundances provides invaluable information for understanding these signaling networks. Currently, mass spectrometry (MS) arguably serves as the most high-throughput and unbiased platform for studying PTMs. Here we detail experimental and analytical procedures for the characterization of lysine acetylation on proteins in general and on histones in particular, which are among the most highly modified proteins in eukaryotic cells.
authors: Department of Molecular Biology, Princeton University, Princeton, NJ, USA.
authors: Barry M
authors: BM
authors: Zee
authors: Benjamin A
authors: BA
authors: Garcia
mesh_terms: D000107:Acetylation; D000818:Animals; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D040901:Proteomics / Q000379:methods*
chemical_list: D006657:Histones; D011506:Proteins; D008239:Lysine
references: Sci Signal. 2009 Nov 17;2(97):pe76
references: 19920250
references: Methods Mol Biol. 2011;717:69-88
references: 21370025
references: Methods Mol Biol. 2009;527:21-9, xi
references: 19241002
references: Nat Protoc. 2008;3(10):1630-8
references: 18833199
references: Nat Biotechnol. 2003 Mar;21(3):255-61
references: 12610572
references: Science. 2009 Aug 14;325(5942):834-40
references: 19608861
references: Cell. 2010 Dec 23;143(7):1174-89
references: 21183079
references: Epigenetics Chromatin. 2010 Dec 06;3(1):22
references: 21134274
references: Mol Cell Proteomics. 2005 Dec;4(12):2010-21
references: 16249172
references: Proteomics. 2003 Jul;3(7):1128-44
references: 12872214