Abstract
Solar ultraviolet radiation (UV) may cause DNA damage. We first report in this study that the large subunit ribosome protein RPL12, from Bomby mori (BmRPL12), participated in UV-induced DNA damage repair. BmRPL12 enhanced the resistance of Escherichia coli (E. coli) to UV radiation and facilitated faster repair of UV-induced DNA damage in silkworm cells. BmRPL12 mainly existed in the cytoplasm in the dimer forms, and the N-terminal nuclear export signal was crucial for the localization of BmRPL12. After UV radiation, BmRPL12 was unable to localize at the UV-induced DNA damage sites to participate in damage repair directly and might indirectly regulate UV-induced DNA damage repair. Our previous research found that BmNPV Bm65 was an important UV damage-induced endonuclease. Here, it was further found that in BmNPV-infected silkworm cells, BmRPL12 in monomeric forms interacted with the virus Bm65 protein only after UV radiation, and BmRPL12 specifically localized at the UV-induced DNA damage sites only in the presence of Bm65. We speculate that after viral infection in cells subjected to UV-induced DNA damage, viral protein Bm65 interacts with BmRPL12 and localizes BmRPL12 to sites of UV-damaged DNA.