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Significance Although human DNA polymerase ζ (Pol ζ) is essential for DNA replication and cell proliferation, difficulties purifying active Pol ζ have hindered its biochemical characterization. We report here the first purification of an active form of human Pol ζ holoenzyme composed of Rev3, Rev7, PolD2, and PolD3, which opens up the possibility for detailed biochemical and structural studies of this essential enzyme. Based on genetic data, it has been postulated that two specialized DNA polymerases are needed for successful translesion synthesis. We show here that human Pol η inserts a nucleotide opposite the lesion, followed by Pol ζ extending the DNA primer; thus, the two complement each other to fully bypass the cisplatin cross-link.

Human Pol ζ purified with accessory subunits is active in translesion DNA synthesis and complements Pol η in cisplatin bypass