Post-translational protein modification represents a fundamental tool within the control of protein functions. While phosphorylation is the longest known of these modifications, several more were identified. Among these, acetylation was originally discovered as an important modification of histones within the process of transcription. Later it was revealed that histone acetylation also plays a crucial role in DNA repair, and that histones are not the only target for transient acetylation within these processes. Although there is no doubt that protein acetylation is essential, its function and even more its regulation is still not fully elucidated. Here we will discuss how protein acetylation occurs within the cellular response to radiation, a well characterized DNA-damaging environmental stressor and further want to draw the attention to open questions within the field of protein acetylation.
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