Cryo-EM structure of translesion DNA synthesis polymerase ζ with a base pair mismatch

Radhika Malik, Robert E. Johnson, Louise Prakash, Satya Prakash, Iban Ubarretxena-Belandia () and Aneel K. Aggarwal ()
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Radhika Malik: Icahn School of Medicine at Mount Sinai, New York
Robert E. Johnson: 301 University Blvd. University of Texas Medical Branch
Louise Prakash: 301 University Blvd. University of Texas Medical Branch
Satya Prakash: 301 University Blvd. University of Texas Medical Branch
Iban Ubarretxena-Belandia: Icahn School of Medicine at Mount Sinai, New York
Aneel K. Aggarwal: Icahn School of Medicine at Mount Sinai, New York

Nature Communications, 2022, vol. 13, issue 1, 1-6

Abstract: Abstract The B-family multi-subunit DNA polymerase ζ (Polζ) is important for translesion DNA synthesis (TLS) during replication, due to its ability to extend synthesis past nucleotides opposite DNA lesions and mismatched base pairs. We present a cryo-EM structure of Saccharomyces cerevisiae Polζ with an A:C mismatch at the primer terminus. The structure shows how the Polζ active site responds to the mismatched duplex DNA distortion, including the loosening of key protein-DNA interactions and a fingers domain in an “open” conformation, while the incoming dCTP is still able to bind for the extension reaction. The structure of the mismatched DNA-Polζ ternary complex reveals insights into mechanisms that either stall or favor continued DNA synthesis in eukaryotes.

Date: 2022
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DOI: 10.1038/s41467-022-28644-7

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