Journal
CELL REPORTS
Volume 10, Issue 9, Pages 1467-1476Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.02.019
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Funding
- Wellcome Trust International Senior Research Fellowship [098022]
- Cancer Research UK
- European Research Council
- Jeantet Foundation
- Foundation for Polish Science Ideas for Poland award
- International Early Career Scientist grant from the Howard Hughes Medical Institute
- European Union [POIG.02.02.00-14-024/08-00]
- Cancer Research UK [11582] Funding Source: researchfish
- The Francis Crick Institute [10216, 10212, 10213] Funding Source: researchfish
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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 alpha 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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