@inbook{0a040750466c4b5e96c3be3054c3e7ba,
title = "Examining histone posttranslational modification patterns by high-resolution mass spectrometry",
abstract = "Histone variants and posttranslational modifications (PTMs) are essential for epigenetic regulation of transcriptional expression. Single and/or combinatorial PTMs of histones play important roles in development and disease formation. Mass spectrometry (MS) has been a powerful tool to study histone variants and PTMs, as it not only can identify novel PTMs but also can provide quantitative measurement of a spectrum of histone variants and PTMs in the same sample. In this chapter, we employ a combination of chemical derivation and high-resolution MS to identify and quantify multiple histone variants and PTMs. Histones are acid extracted and modified with propionyl groups and subsequently produces suitable sizes of fragments for MS analysis by trypsin digestion. The newly generated N-termini of histone peptides can be differentially marked by stable isotope labeling in a second reaction of propionylation, which enables direct comparison between two different samples in the following MS analysis.",
keywords = "Epigenetics, High-performance liquid chromatography, Histone posttranslational modifications, Mass spectrometry, Propionylation, Stable isotope labeling",
author = "Shu Lin and Garcia, {Benjamin A.}",
note = "Funding Information: We thank Barry Zee and Natarajan V. Bhanu for providing example data. This work is supported by a National Science Foundation (NSF) Early Faculty CAREER award, an NIH Innovator award (DP2OD007447) from the Office of the Director, National Institutes of Health, and an NSF grant (CBET-0941143) to B. A. G. and S. L. is supported by a postdoctoral training grant from the Center for Quantitative Biology, Princeton University. This work is also supported by an NIGMS P50GM071508 grant to the Lewis-Sigler Institute (PI D. Botstein).",
year = "2012",
doi = "10.1016/B978-0-12-391940-3.00001-9",
language = "English",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "3--28",
booktitle = "Methods in Enzymology",
}