Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction
Gurunathan Laxmikanthan,
Chen Xu,
Axel F Brilot,
David Warren,
Lindsay Steele,
Nicole Seah,
Wenjun Tong,
Nikolaus Grigorieff,
Arthur Landy,
Gregory D Van Duyne
Affiliations
Gurunathan Laxmikanthan
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
Chen Xu
Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States
Axel F Brilot
Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States
David Warren
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
Lindsay Steele
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
Nicole Seah
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
Wenjun Tong
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States; Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States
Arthur Landy
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United States
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.
