TY - JOUR
T1 - The Architecture of Yeast DNA Polymerase ζ
AU - Gómez-Llorente, Yacob
AU - Malik, Radhika
AU - Jain, Rinku
AU - Choudhury, Jayati Roy
AU - Johnson, Robert E.
AU - Prakash, Louise
AU - Prakash, Satya
AU - Ubarretxena-Belandia, Iban
AU - Aggarwal, Aneel K.
N1 - Funding Information:
Access to electron microscopy instrumentation was provided by the New York Structural Biology Center, a STAR center supported by the New York State Office of Science, Technology, and Academic Research. Computing resources needed for this work were provided in part by the scientific computing facility of the Icahn School of Medicine at Mount Sinai. L.P. was supported by grant CA107650 from the National Institutes of Health.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2013/10/17
Y1 - 2013/10/17
N2 - 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
AB - 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
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U2 - 10.1016/j.celrep.2013.08.046
DO - 10.1016/j.celrep.2013.08.046
M3 - Article
C2 - 24120860
AN - SCOPUS:84885850190
VL - 5
SP - 79
EP - 86
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 1
ER -