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Protein acetylation was initially recognized as an essential post-translational modification of histones in the course of transcription and DNA repair [1]. Lately, even so, the arena of acetylation has been extended to include things like non-histone proteins, particularly those involved within the approach of DNA double strand break (DSB) repair [2]. In truth, it has been not too long ago demonstrated that acetylation regulates the important DNA harm response kinases ATM and DNA-PKcs [2,4], at the same time as a plethora of DNA repair elements which includes NBS1, Ku70, and p53 [3,6]. These evidences have a tendency to assistance a pivotal part for acetylation in the process of DNA damage response and repair–ostensibly through facilitating the recognition and signaling of DNA lesions, at the same time as orchestrating protein interactions to recruit activities necessary inside the method with the repair. Especially, acetylation is critical in the activation of DNA damage response pathways [2,4]. In spite of these advances, precise functional roles of acetylation on the most non-histone DNA repair proteins are nevertheless elusive. Current study suggests that this covalent protein post-translational modification could also confer new functional properties, and thus modified proteins can carry out distinct roles. Indeed, it has been nicely documented that Ku70 and p53 acetylation are involved in promoting apoptosis [6,8,10]. Although p53 and Ku70 interaction is acetylation-independent, p53 acety.
