In Vitro Histone Deacetylase Activity Screening: Making a Case for Better Assays

Quaovi H. Sodji*, James R. Kornacki, Milan Mrksich, Adegboyega K. Oyelere

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


Recent advances in epigenetics and proteomics have emphasized the importance of protein acetylation and deacetylation in cellular homeostasis. Dynamic control of the acetylation states, by two functionally opposing enzymes - histone deacetylase (HDAC) and histone acetyltransferase (HAT) - has emerged as a key regulatory mechanism for more than 2000 proteins. HDAC-mediated disregulation of the protein deacetylation has been linked to various diseases, including cancer. Deconvoluting the collective and individual roles of HDAC isoforms, especially as they pertain to human pathological states, continues to be a focus for both academic and pharmaceutical laboratories. However, limitations of current HDAC activity assays temper progress in this growing field. In this chapter, we review various HDAC activity assays that have been developed, highlighting the strengths and weaknesses of each assay. We conclude by making a case for substrate-matched, label-free in vitro assays as desirable alternatives to the commonly used fluorescence-based HDAC activity assays.

Original languageEnglish (US)
Title of host publicationEpigenetic Technological Applications
PublisherElsevier Inc
Number of pages14
ISBN (Electronic)9780128013274
ISBN (Print)9780128010808
StatePublished - Jun 17 2015


  • Acetylation
  • Deacetylation
  • HDAC
  • Histone deacetylase
  • Protein acetylation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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