文摘
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Summary
DNA polymerase 味 (Pol味) is specialized for the extension step of translesion DNA synthesis (TLS). Despite its central role in maintaining genome integrity, little is known about its overall architecture. Initially identified as a heterodimer of the catalytic subunit Rev3 and the accessory subunit Rev7, yeast Pol味 has recently been shown to form a stable four-subunit enzyme (Pol味-d) upon the incorporation of Pol31 and Pol32, the accessory subunits of yeast Pol未. To understand the 3D architecture and assembly of Pol味 and Pol味-d, we employed electron microscopy. We show here how the catalytic and accessory subunits of Pol味 and Pol味-d are organized relative to each other. In particular, we show that Pol味-d has a bilobal architecture resembling the replicative polymerases and that Pol32 lies in proximity to Rev7. Collectively, our study provides views of Pol味 and Pol味-d and a structural framework for understanding their roles in DNA damage bypass.
