@inbook{3e0aee667a8f4767a919bf9972818c11,
title = "Biochemical and cellular assays to assess the effects of acetylation on base excision repair enzymes",
abstract = "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.",
keywords = "APE1, Acetylation, BER, Colony formation assay, Comet assay, DNA damage, DNA repair assay, EMSA, In vitro acetylation",
author = "Shrabasti Roychoudhury and Suravi Pramanik and Harris, {Hannah L.} and Bhakat, {Kishor K.}",
note = "Publisher Copyright: {\textcopyright} Springer Science+Business Media, LLC, part of Springer Nature 2019.",
year = "2019",
doi = "10.1007/978-1-4939-9434-2_11",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "191--206",
booktitle = "Methods in Molecular Biology",
}