Bioanalytical approaches for the detection of protein acetylation-related enzymes

Anal Bioanal Chem. 2016 Apr;408(11):2659-68. doi: 10.1007/s00216-016-9304-7. Epub 2016 Jan 21.

Abstract

Reversible protein acetylation catalyzed by histone acetyltransferases (HATs) and histone deacetylases (HDACs) is an essential post-translational modification (PTM) mechanism which correlates largely with epigenetic gene regulation such as transcriptional activation, DNA replication, histone deposition, and DNA repair. Dysfunction of histone acetylation and the aberrant activity of HATs/HDACs is often associated with the pathogenesis of numerous diseases, especially cancer. Therefore, developing potent and specific analytical methods for HATs/HDACs is important for fundamental biochemical research, disease diagnosis and treatment, and drug development. This paper briefly summarizes the general design strategies used in HAT/HDAC sensors, gives a systematic overview of recent advances in the analytical methods for HAT/HDAC enzymatic analysis, classifies these methods by their biorecognition mechanisms and relative applications either in vitro or in living cells, then outlines challenges faced by these bioanalytical methods and offers perspectives on future developments.

Keywords: Acetyltransferase and deacetylase; Analytical method; Drug screening; Protein acetylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Binding, Competitive
  • Biosensing Techniques
  • Histone Acetyltransferases / metabolism*
  • Histone Deacetylases / metabolism*
  • Proteins / metabolism*

Substances

  • Proteins
  • Histone Acetyltransferases
  • Histone Deacetylases