Publication Abstract from PubMed
Holliday junctions occur as intermediates in homologous recombination and DNA repair. In bacteria, resolution of Holliday junctions is accomplished by the RuvABC system, consisting of a junction-specific helicase complex RuvAB, which promotes branch migration, and a junction-specific endonuclease RuvC, which nicks two strands. The crystal structure of a complex between the RuvA protein of M. leprae and a synthetic four-way junction has now been determined. Rather than binding on the open surface of a RuvA tetramer as previously suggested, the DNA is sandwiched between two RuvA tetramers, which form a closed octameric shell, stabilized by a conserved tetramer-tetramer interface. Interactions between the DNA backbone and helix-hairpin-helix motifs from both tetramers suggest a mechanism for strand separation promoted by RuvA.
Crystal structure of an octameric RuvA-Holliday junction complex.,Roe SM, Barlow T, Brown T, Oram M, Keeley A, Tsaneva IR, Pearl LH Mol Cell. 1998 Sep;2(3):361-72. PMID:9774974[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
