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The architecture of yeast DNA polymerase zeta (927.2)
Author(s) -
Malik Radhika,
Llorente Yacob,
Jain Rinku,
Choudhary Jayati,
Johnson Robert,
Prakash Louise,
Prakash Satya,
UbarretxenaBelandia Iban,
Aggarwal Aneel
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.927.2
Subject(s) - protein subunit , dna polymerase , polymerase , yeast , dna , biology , saccharomyces cerevisiae , processivity , microbiology and biotechnology , biochemistry , gene
DNA polymerase ζ (Polζ) is a multi‐subunit enzyme that 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 homodimer of the catalytic subunit Rev3 and the accessory subunit Rev7, yeast Polζ has recently been shown to also form a stable four‐subunit enzyme (Polζ‐d) upon incorporation of Pol31 and Pol32, the accessory subunits of yeast Polδ. To understand the 3‐D architecture and assembly of Polζ and Polζ‐d we employed electron microscopy (EM). 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 the first views of Polζ and Polζ‐d, and a structural framework for understanding their roles in DNA damage bypass.