Branched DNA structures that occur during DNA repair and recombination must be efficiently processed by structure-specific endonucleases in order to avoid cell death. In the present paper, we summarize our screen for new interaction partners for the archaeal replication clamp that led to the functional characterization of a novel endonuclease family, dubbed NucS. Structural analyses of Pyrococcus abyssi NucS revealed an unexpected binding site for ssDNA (single-stranded DNA) that directs, together with the replication clamp, the nuclease activity of this protein towards ssDNA–dsDNA (double-stranded DNA) junctions. Our studies suggest that understanding the detailed architecture and dynamic behaviour of the NucS (nuclease specific for ssDNA)–PCNA (proliferating-cell nuclear antigen) complex with DNA will be crucial for identification of its physiologically relevant activities.
Structure and function of a novel endonuclease acting on branched DNA substrates
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Christophe Creze, Roxane Lestini, Joelle Kühn, Alessio Ligabue, Hubert F. Becker, Mirjam Czjzek, Didier Flament, Hannu Myllykallio; Structure and function of a novel endonuclease acting on branched DNA substrates. Biochem Soc Trans 1 February 2011; 39 (1): 145–149. doi: https://doi.org/10.1042/BST0390145
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