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

eLife

Nikolaus Grigorieff¹  Nicole Seah¹  Chen Xu¹  Gregory D Van Duyne¹  Axel F Brilot²  David Warren²  Arthur Landy³  Gurunathan Laxmikanthan³  Lindsay Steele³  Wenjun Tong³ 

[1] Division of Biology and Medicine, Brown University, Providence, United States;Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States;Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States;

关键词: site-specific recombination;    bacteriophage lambda;    electron cryo-microscopy;    viral excision;    viral integration;   

DOI  :  10.7554/eLife.14313

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown