Open AccessBreaking Up Just Got Easier to Do
Author(s) -
Hannah L. Klein,
Lorraine S. Symington
Publication year - 2009
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2009.06.039
Subject(s) - holliday junction , biology , endonuclease , cleavage (geology) , restriction enzyme , computational biology , genetics , microbiology and biotechnology , dna , homologous recombination , paleontology , fracture (geology)
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.
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