Breaking up just got easier to do.
The SLX4 protein functions as a platform for catalytic subunits of structure-specific endonucleases. Findings reported in Cell (Fekairi et al., 2009; Svendsen et al., 2009) and in Molecular Cell (Andersen et al., 2009; Muñoz et al., 2009) now identify the human SLX4 and show that in association with the SLX1 endonuclease it directs the symmetric cleavage and resolution of Holliday junctions.
Klein
Hannah L
HL
Department of Biochemistry, New York University Langone Medical Center, 550 First Avenue, New York, NY 10016, USA. hannah.klein@nyumc.org
Symington
Lorraine S
LS
D000818:Animals; D002875:Chromosomes / Q000378:metabolism*; D004260:DNA Repair; D045566:DNA, Cruciform / Q000378:metabolism*; D045565:Holliday Junction Resolvases / Q000302:isolation & purification*; D006801:Humans; D009690:Nucleic Acid Conformation; D011995:Recombination, Genetic
D045566:DNA, Cruciform; D045565:Holliday Junction Resolvases