Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction
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...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-05-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/14313 |
| _version_ | 1811227870866964480 |
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| author | Gurunathan Laxmikanthan Chen Xu Axel F Brilot David Warren Lindsay Steele Nicole Seah Wenjun Tong Nikolaus Grigorieff Arthur Landy Gregory D Van Duyne |
| author_facet | Gurunathan Laxmikanthan Chen Xu Axel F Brilot David Warren Lindsay Steele Nicole Seah Wenjun Tong Nikolaus Grigorieff Arthur Landy Gregory D Van Duyne |
| author_sort | Gurunathan Laxmikanthan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T09:48:00Z |
| format | Article |
| id | doaj.art-c2dcf8cc9a88456b8a97f71a3655d550 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T09:48:00Z |
| publishDate | 2016-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-c2dcf8cc9a88456b8a97f71a3655d5502022-12-22T03:37:53ZengeLife Sciences Publications LtdeLife2050-084X2016-05-01510.7554/eLife.14313Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transactionGurunathan Laxmikanthan0Chen Xu1Axel F Brilot2David Warren3Lindsay Steele4Nicole Seah5Wenjun Tong6Nikolaus Grigorieff7https://orcid.org/0000-0002-1506-909XArthur Landy8Gregory D Van Duyne9https://orcid.org/0000-0003-0247-1626Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United StatesDepartment of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United StatesDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States; Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United StatesDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, United States; Division of Biology and Medicine, Brown University, Providence, United StatesDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United StatesThe 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.https://elifesciences.org/articles/14313site-specific recombinationbacteriophage lambdaelectron cryo-microscopyviral excisionviral integration |
| spellingShingle | Gurunathan Laxmikanthan Chen Xu Axel F Brilot David Warren Lindsay Steele Nicole Seah Wenjun Tong Nikolaus Grigorieff Arthur Landy Gregory D Van Duyne Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction eLife site-specific recombination bacteriophage lambda electron cryo-microscopy viral excision viral integration |
| title | Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction |
| title_full | Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction |
| title_fullStr | Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction |
| title_full_unstemmed | Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction |
| title_short | Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction |
| title_sort | structure of a holliday junction complex reveals mechanisms governing a highly regulated dna transaction |
| topic | site-specific recombination bacteriophage lambda electron cryo-microscopy viral excision viral integration |
| url | https://elifesciences.org/articles/14313 |
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