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• W2176090941 abstract "The Dna2 nuclease-helicase maintains genomic integrity by processing DNA double-strand breaks, Okazaki fragments and stalled replication forks. Dna2 requires ssDNA ends, and is dependent on the ssDNA-binding protein Rpa, which controls cleavage polarity. Here we present the 2.3 Å structure of intact mouse Dna2 bound to a 15-nucleotide ssDNA. The nuclease active site is embedded in a long, narrow tunnel through which the DNA has to thread. The helicase domain is required for DNA binding but not threading. We also present the structure of a flexibly-tethered Dna2-Rpa interaction that recruits Dna2 to Rpa-coated DNA. We establish that a second Dna2-Rpa interaction is mutually exclusive with Rpa-DNA interactions and mediates the displacement of Rpa from ssDNA. This interaction occurs at the nuclease tunnel entrance and the 5' end of the Rpa-DNA complex. Hence, it only displaces Rpa from the 5' but not 3' end, explaining how Rpa regulates cleavage polarity." @default.
• W2176090941 created "2016-06-24" @default.
• W2176090941 creator A5018371071 @default.
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• W2176090941 date "2015-11-02" @default.
• W2176090941 modified "2023-10-03" @default.
• W2176090941 title "Dna2 nuclease-helicase structure, mechanism and regulation by Rpa" @default.
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• W2176090941 doi "https://doi.org/10.7554/elife.09832" @default.
• W2176090941 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4716839" @default.
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• W2176090941 hasPublicationYear "2015" @default.
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