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Elife. 2016 May 25;5. pii: e14313. doi: 10.7554/eLife.14313.

Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction.

Author information

1
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States.
2
Division of Biology and Medicine, Brown University, Providence, United States.
3
Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States.
4
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
5
Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States.

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.

KEYWORDS:

E. coli; bacteriophage lambda; biophysics; chromosomes; electron cryo-microscopy; genes; site-specific recombination; structural biology; viral excision; viral integration

PMID:
27223329
PMCID:
PMC4880445
DOI:
10.7554/eLife.14313
[Indexed for MEDLINE]
Free PMC Article

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