Abstract
Translesion DNA synthesis (TLS) by Y‐family polymerases has been well studies in recent years. These enzymes differ from replicative polymerases by possessing a spacious pre‐formed active site. They can physically accommodate a variety of DNA lesions and facilitate their bypass. Each Y‐family DNA polymerase has a unique binding pocket for the replicating base pair and thereby has preference for specific lesions to bypass or distinct non‐Watson‐Crick base pairs to make. Interestingly, several B‐family DNA polymerases are involved in translesion and mutagenic DNA synthesis, for example E. coli pol II and eukaryotic pol zeta (Rev3‐Rev7). According to amino acid sequence and three‐dimensional structure, these TLS polymerases are highly similar to the replicative polymerases in the same family. It is so far unknown what makes these B‐family DNA polymerase mutagenic and capable of TLS. I will present our recent structural and biochemical analyses of E. coli pol II, which shed light on the mechanism for a replicative‐like polymerase to carry out TLS.
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