Biochemical and cellular assays to assess the effects of acetylation on base excision repair enzymes

Shrabasti Roychoudhury, Suravi Pramanik, Hannah L. Harris, Kishor K. Bhakat

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


Protein posttranslational modifications (PTMs), including acetylation, have emerged as important regulators for controlling many cellular processes. DNA base excision repair (BER), a highly coordinated multistep cellular process, is primarily involved in the repair of both endogenous and drug-induced exogenous DNA base damages. BER relies on sequential recruitment and coordinated actions of multiple proteins. Increasing evidence suggests that acetylation of lysine residues of BER proteins facilitates fine-tuning of enzymatic activities, protein-protein interactions, and coordination of the steps in BER pathway. In this chapter, we describe detailed in vitro and in vivo approaches to examine the effect of acetylation on BER enzymes, focusing on the impact of acetylation of AP-endonuclease (APE1), a key enzyme in BER pathway, on its DNA damage repair activity, substrate-binding, and subcellular localization.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages16
StatePublished - 2019

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • APE1
  • Acetylation
  • BER
  • Colony formation assay
  • Comet assay
  • DNA damage
  • DNA repair assay
  • EMSA
  • In vitro acetylation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


Dive into the research topics of 'Biochemical and cellular assays to assess the effects of acetylation on base excision repair enzymes'. Together they form a unique fingerprint.

Cite this