title: Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction.
abstract: The molecular machinery responsible for DNA expression, recombination, and compaction has been difficult to visualize as functionally complete entities due to their combinatorial and structural complexity. We report here the structure of the intact functional assembly responsible for regulating and executing a site-specific DNA recombination reaction. The assembly is a 240-bp Holliday junction (HJ) bound specifically by 11 protein subunits. This higher-order complex is a key intermediate in the tightly regulated pathway for the excision of bacteriophage λ viral DNA out of the E. coli host chromosome, an extensively studied paradigmatic model system for the regulated rearrangement of DNA. Our results provide a structural basis for pre-existing data describing the excisive and integrative recombination pathways, and they help explain their regulation.
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: Gurunathan
authors.initials: G
authors.lastname: Laxmikanthan
authors.affiliation: Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States.
authors.forename: Chen
authors.initials: C
authors.lastname: Xu
authors.affiliation: Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States.
authors.forename: Axel F
authors.initials: AF
authors.lastname: Brilot
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: David
authors.initials: D
authors.lastname: Warren
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: Lindsay
authors.initials: L
authors.lastname: Steele
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: Nicole
authors.initials: N
authors.lastname: Seah
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: Wenjun
authors.initials: W
authors.lastname: Tong
authors.affiliation: Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States.|Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
authors.forename: Nikolaus
authors.identifier: 0000-0002-1506-909X
authors.initials: N
authors.lastname: Grigorieff
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.|Division of Biology and Medicine, Brown University, Providence, United States.
authors.forename: Arthur
authors.initials: A
authors.lastname: Landy
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States.
authors.forename: Gregory D
authors.identifier: 0000-0003-0247-1626
authors.initials: GD
authors.lastname: Van Duyne
mesh_terms: D010582:Bacteriophage lambda / Q000235:genetics*; D020285:Cryoelectron Microscopy; D004269:DNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D045566:DNA, Cruciform / Q000737:chemistry*; D004279:DNA, Viral / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D021621:Imaging, Three-Dimensional; D008958:Models, Molecular; D011995:Recombination, Genetic
chemical_list: D004269:DNA, Bacterial; D045566:DNA, Cruciform; D004279:DNA, Viral; D029968:Escherichia coli Proteins
keywords: E. coli; bacteriophage lambda; biophysics; chromosomes; electron cryo-microscopy; genes; site-specific recombination; structural biology; viral excision; viral integration