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TitleStructure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction.
Journal, issue, pagesElife, Vol. 5, Year 2016
Publish dateMay 25, 2016
AuthorsGurunathan Laxmikanthan / Chen Xu / Axel F Brilot / David Warren / Lindsay Steele / Nicole Seah / Wenjun Tong / Nikolaus Grigorieff / Arthur Landy / Gregory D Van Duyne /
PubMed AbstractThe molecular machinery responsible for DNA expression, recombination, and compaction has been difficult to visualize as functionally complete entities due to their combinatorial and structural ...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.
External linksElife / PubMed:27223329 / PubMed Central
MethodsEM (single particle)
Resolution11.0 Å
Structure data

3400

5j0n

EMDB-3400, PDB-5j0n:
Lambda excision HJ intermediate
Method: EM (single particle) / Resolution: 11.0 Å

Source
  • enterobacteria phage lambda (virus)
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / HYDROLASE/DNA / bacteriophage lambda / excision / site-specific recombination / Holliday junction / HYDROLASE-DNA complex

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