Methods for analyzing histone citrullination in chromatin structure and gene regulation

Pingxin Li, Jing Hu, Yanming Wang

Research output: Chapter in Book/Report/Conference proceedingChapter

9 Scopus citations


Histone posttranslational modifications play significant roles in regulating chromatin structure and gene expression. One of the histone modifications, histone citrullination, is catalyzed by an enzyme called peptidylarginine deiminase 4 (PAD4, also called PADI4), which converts both histone arginine (Arg) and mono-methyl arginine residues to citrulline. Recent studies have found that histone citrullination counteracts the effect of histone arginine methylation and functions as a repressive marker to turn off gene expression. Here, we describe assays to study histone citrullination by PAD4 in vitro and in vivo. We also describe approaches to measure histone citrullination levels at gene promoters using chromatin immunoprecipitation assay and analyze the effects of PAD4 inhibitor on cell cycle and apoptosis by flow cytometry. These methods would be useful techniques to study this unique histone modification.

Original languageEnglish (US)
Title of host publicationTranscriptional Regulation
Subtitle of host publicationMethods and Protocols
EditorsAles Vancura
Number of pages16
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics


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