7s0t: Difference between revisions
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The B-family multi-subunit DNA polymerase zeta (Polzeta) 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 Polzeta with an A:C mismatch at the primer terminus. The structure shows how the Polzeta 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-Polzeta ternary complex reveals insights into mechanisms that either stall or favor continued DNA synthesis in eukaryotes. | The B-family multi-subunit DNA polymerase zeta (Polzeta) 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 Polzeta with an A:C mismatch at the primer terminus. The structure shows how the Polzeta 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-Polzeta ternary complex reveals insights into mechanisms that either stall or favor continued DNA synthesis in eukaryotes. | ||
, PMID:35217661<ref>PMID:35217661</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
