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  Structural rearrangements in the phage head-to-tail interface during assembly and infection

Chaban, Y., Lurz, R., Brasilès, S., Cornilleau, C., Karreman, M., Zinn-Justin, S., et al. (2015). Structural rearrangements in the phage head-to-tail interface during assembly and infection. Proceedings of the National Academy of Sciences of the United States of America, 112(22), 7009-7014. doi:10.1073/pnas.1504039112.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A788-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A789-B
Genre: Journal Article

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 Creators:
Chaban, Yuriy 1, Author
Lurz, Rudolf2, Author              
Brasilès, Sandrine3, 4, Author
Cornilleau, Charlène 4, Author
Karreman, Matthia 1, 5, Author
Zinn-Justin, Sophie6, Author
Tavares, Paulo3, 4, Author
Orlova, Elena V. 1, Author
Affiliations:
1Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, United Kingdom, ou_persistent22              
2Imaging/Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Department of Virology, Institute for Integrative Biology of the Cell (I2BC), UMR 9198 CEA, CNRS, Universitè Paris-Sud, Campus CNRS, 91198 Gif-sur-Yvette cedex, France, ou_persistent22              
4Laboratory of Molecular and Structural Virology (VMS), UPR3296 CNRS, Campus CNRS, 91198 Gif-sur-Yvette cedex, France, ou_persistent22              
5European Molecular Biology Laboratory, 69117 Heidelberg, Germany, ou_persistent22              
6Department of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), UMR 9198 CEA, CNRS, Universitè Paris-Sud, Campus CEA, Saclay, 91191 Gif-sur-Yvette cedex, France , ou_persistent22              

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Free keywords: DNA gatekeeper, viral infection, bacteriophage, allosteric mechanism, hybrid methods
 Abstract: Many icosahedral viruses use a specialized portal vertex to control genome encapsidation and release from the viral capsid. In tailed bacteriophages, the portal system is connected to a tail structure that provides the pipeline for genome delivery to the host cell. We report the first, to our knowledge, subnanometer structures of the complete portal–phage tail interface that mimic the states before and after DNA release during phage infection. They uncover structural rearrangements associated with intimate protein–DNA interactions. The portal protein gp6 of bacteriophage SPP1 undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA. A network of protein–protein interactions primes consecutive binding of proteins gp15 and gp16 to extend and close the channel. This critical step that prevents genome leakage from the capsid is achieved by a previously unidentified allosteric mechanism: gp16 binding to two different regions of gp15 drives correct positioning and folding of an inner gp16 loop to interact with equivalent loops of the other gp16 subunits. Together, these loops build a plug that closes the channel. Gp16 then fastens the tail to yield the infectious virion. The gatekeeper system opens for viral genome exit at the beginning of infection but recloses afterward, suggesting a molecular diaphragm-like mechanism to control DNA efflux. The mechanisms described here, controlling the essential steps of phage genome movements during virus assembly and infection, are likely to be conserved among long-tailed phages, the largest group of viruses in the Biosphere.

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Language(s): eng - English
 Dates: 2015-05-192015-06-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1073/pnas.1504039112
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 112 (22) Sequence Number: - Start / End Page: 7009 - 7014 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230