Significance Repair of the majority of UV-induced DNA damage in mammalian cells by the nucleotide excision repair pathway starts with rapid recruitment of Xeroderma pigmentosum C (XPC) protein to the lesion. However, rapidity of XPC recruitment to the lesion site in a genomic context cannot be fully explained by the known properties of XPC or its partner protein DDB2. Here, we show that the DNA damage-detecting nuclear protein PARP1 forms a stable complex with XPC before DNA damage and transfers it very rapidly to the DNA lesion site if other repair conditions are present. Since PARP1 is known to interact with many proteins under steady-state conditions, our results reveal a paradigm that an association with PARP1 could confer a functional advantage to these proteins.