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Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel
The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4755594/ https://www.ncbi.nlm.nih.gov/pubmed/26882199 http://dx.doi.org/10.1371/journal.pone.0149337 |
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author | Zhao, Haiyan Speir, Jeffrey A. Matsui, Tsutomu Lin, Zihan Liang, Lingfei Lynn, Anna Y. Varnado, Brittany Weiss, Thomas M. Tang, Liang |
author_facet | Zhao, Haiyan Speir, Jeffrey A. Matsui, Tsutomu Lin, Zihan Liang, Lingfei Lynn, Anna Y. Varnado, Brittany Weiss, Thomas M. Tang, Liang |
author_sort | Zhao, Haiyan |
collection | PubMed |
description | The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. The gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device. |
format | Online Article Text |
id | pubmed-4755594 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-47555942016-02-26 Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel Zhao, Haiyan Speir, Jeffrey A. Matsui, Tsutomu Lin, Zihan Liang, Lingfei Lynn, Anna Y. Varnado, Brittany Weiss, Thomas M. Tang, Liang PLoS One Research Article The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. The gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device. Public Library of Science 2016-02-16 /pmc/articles/PMC4755594/ /pubmed/26882199 http://dx.doi.org/10.1371/journal.pone.0149337 Text en © 2016 Zhao et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Zhao, Haiyan Speir, Jeffrey A. Matsui, Tsutomu Lin, Zihan Liang, Lingfei Lynn, Anna Y. Varnado, Brittany Weiss, Thomas M. Tang, Liang Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title | Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title_full | Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title_fullStr | Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title_full_unstemmed | Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title_short | Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel |
title_sort | structure of a bacterial virus dna-injection protein complex reveals a decameric assembly with a constricted molecular channel |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4755594/ https://www.ncbi.nlm.nih.gov/pubmed/26882199 http://dx.doi.org/10.1371/journal.pone.0149337 |
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