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Protein acetylation was originally recognized as an important post-translational IRAK4 Species modification of histones in the course of transcription and DNA repair [1]. Recently, nonetheless, the arena of acetylation has been extended to consist of non-histone proteins, specifically those involved inside the approach of DNA double strand break (DSB) repair [2]. In reality, it has been recently demonstrated that acetylation regulates the crucial DNA damage response kinases ATM and DNA-PKcs [2,4], as well as a plethora of DNA repair variables which includes NBS1, Ku70, and p53 [3,6]. These evidences tend to assistance a pivotal role for acetylation in the approach of DNA harm response and repair–ostensibly through facilitating the recognition and signaling of DNA lesions, too as orchestrating protein interactions to recruit activities necessary within the process in the repair. Particularly, acetylation is crucial within the activation of DNA damage response pathways [2,4]. In spite of those advances, precise functional roles of acetylation on the most non-histone DNA repair proteins are nevertheless elusive. Current investigation suggests that this covalent protein post-translational modification could a.