Fig. 3
From: Emerging roles of non-histone protein crotonylation in biomedicine
The role of RPA1 Kcr in camptothecin (CPT)-induced double-strand break (DSB) of DNA. RPA1 takes an important role in DNA repair. The Kcr levels at K88, K379, and K595 sites of RPA1 are upregulated by DNA damage but downregulated by CDYL. Sites K379 and K595 locate at the DNA binding domain of RPA1 and may be more important than site K88 for the ssDNA binding ability of RPA1. Crotonylation of RPA1 promotes the binding of RPA1 to ssDNA, recruits RPA1 to the site of DNA damage, enhances the interaction of RPA1 with homologous recombination (HR) factors (including BLM, DNA2L, Mre11, NBS1, and RAD51), and promotes the formation of RAD51 lesions after CPT injury. As a result, the Kcr of RPA1 may make the cells survive and resistant to apoptosis after DNA damage (referenced to: Yu H et al. (2020) Sci Adv 6:eaay4697)