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Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. 2015

Vineet Gaur, and Haley D M Wyatt, and Weronika Komorowska, and Roman H Szczepanowski, and Daniele de Sanctis, and Karolina M Gorecka, and Stephen C West, and Marcin Nowotny
Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, 4 Księcia Trojdena Street, 02-109 Warsaw, Poland.

The SLX1-SLX4 endonuclease required for homologous recombination and DNA repair in eukaryotic cells cleaves a variety of branched DNA structures. The nuclease subunit SLX1 is activated by association with a scaffolding protein SLX4. At the present time, little is known about the structure of SLX1-SLX4 or its mechanism of action. Here, we report the structural insights into SLX1-SLX4 by detailing the crystal structure of Candida glabrata (Cg) Slx1 alone and in combination with the C-terminal region of Slx4. The structure of Slx1 reveals a compact arrangement of the GIY-YIG nuclease and RING domains, which is reinforced by a long α helix. Slx1 forms a stable homodimer that blocks its active site. Slx1-Slx4 interaction is mutually exclusive with Slx1 homodimerization, suggesting a mechanism for Slx1 activation by Slx4.

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