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TransLesion Synthesis (TLS) is a DNA damage tolerance mechanism that allows continued DNA synthesis, even in the presence of damaged DNA templates. In response to DNA damage, TLS polymerases are recruited to replication forks via interactions with ubiquitinated Proliferating Cell Nuclear Antigen (PCNA) involving PCNA-interacting protein box (PIP-box) and ubiquitin-binding domains (UBDs). We now report the first crystal structures of human PCNA in complex with three TLS polymerase peptides containing the non-canonical PIP-box. TLS polymerases interact with PCNA in different ways, both from one another and from canonical PIP-box peptides. Furthermore, we discuss these TLS polymerases interact with ubiquitinated PCNA.

Structural Basis for Novel Interactions between Human TLS Polymerases and PCNA