| Literature DB >> 24120860 |
Yacob Gómez-Llorente1, Radhika Malik, Rinku Jain, Jayati Roy Choudhury, Robert E Johnson, Louise Prakash, Satya Prakash, Iban Ubarretxena-Belandia, Aneel K Aggarwal.
Abstract
DNA polymerase ζ (Polζ) 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 Polζ has recently been shown to form a stable four-subunit enzyme (Polζ-d) upon the incorporation of Pol31 and Pol32, the accessory subunits of yeast Polδ. To understand the 3D architecture and assembly of Polζ and Polζ-d, we employed electron microscopy. We show here how the catalytic and accessory subunits of Polζ and Polζ-d are organized relative to each other. In particular, we show that Polζ-d has a bilobal architecture resembling the replicative polymerases and that Pol32 lies in proximity to Rev7. Collectively, our study provides views of Polζ and Polζ-d and a structural framework for understanding their roles in DNA damage bypass.Entities:
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Year: 2013 PMID: 24120860 PMCID: PMC3883112 DOI: 10.1016/j.celrep.2013.08.046
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423