The C-terminal Domain of Human Rev1 Contains Independent Binding Sites for DNA Polymerase η and Rev7 Subunit of Polymerase ζ

摘要

Human Rev1 is a translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap-filling. Rev1 plays an essential structural role in TLS by providing a binding platform for other TLS polymerases that insert nucleotides across DNA lesions (polη, polι, polκ) and extend the distorted primer-terminus (polζ). We use NMR spectroscopy to demonstrate that the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' polη and Rev7 subunit of the 'extender' polζ, thereby serving as a cassette that may accommodate several polymerases making them instantaneously available for TLS.