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Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands
Staphylococcus aureus pathogenicity islands (SaPIs), such as SaPI1, exploit specific helper bacteriophages, like 80α, for their high frequency mobilization, a process termed ‘molecular piracy’. SaPI1 redirects the helper’s assembly pathway to form small capsids that can only accommodate the smaller...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5644958/ https://www.ncbi.nlm.nih.gov/pubmed/28984245 http://dx.doi.org/10.7554/eLife.30822 |
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author | Dearborn, Altaira D Wall, Erin A Kizziah, James L Klenow, Laura Parker, Laura K Manning, Keith A Spilman, Michael S Spear, John M Christie, Gail E Dokland, Terje |
author_facet | Dearborn, Altaira D Wall, Erin A Kizziah, James L Klenow, Laura Parker, Laura K Manning, Keith A Spilman, Michael S Spear, John M Christie, Gail E Dokland, Terje |
author_sort | Dearborn, Altaira D |
collection | PubMed |
description | Staphylococcus aureus pathogenicity islands (SaPIs), such as SaPI1, exploit specific helper bacteriophages, like 80α, for their high frequency mobilization, a process termed ‘molecular piracy’. SaPI1 redirects the helper’s assembly pathway to form small capsids that can only accommodate the smaller SaPI1 genome, but not a complete phage genome. SaPI1 encodes two proteins, CpmA and CpmB, that are responsible for this size redirection. We have determined the structures of the 80α and SaPI1 procapsids to near-atomic resolution by cryo-electron microscopy, and show that CpmB competes with the 80α scaffolding protein (SP) for a binding site on the capsid protein (CP), and works by altering the angle between capsomers. We probed these interactions genetically and identified second-site suppressors of lethal mutations in SP. Our structures show, for the first time, the detailed interactions between SP and CP in a bacteriophage, providing unique insights into macromolecular assembly processes. |
format | Online Article Text |
id | pubmed-5644958 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-56449582017-10-23 Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands Dearborn, Altaira D Wall, Erin A Kizziah, James L Klenow, Laura Parker, Laura K Manning, Keith A Spilman, Michael S Spear, John M Christie, Gail E Dokland, Terje eLife Structural Biology and Molecular Biophysics Staphylococcus aureus pathogenicity islands (SaPIs), such as SaPI1, exploit specific helper bacteriophages, like 80α, for their high frequency mobilization, a process termed ‘molecular piracy’. SaPI1 redirects the helper’s assembly pathway to form small capsids that can only accommodate the smaller SaPI1 genome, but not a complete phage genome. SaPI1 encodes two proteins, CpmA and CpmB, that are responsible for this size redirection. We have determined the structures of the 80α and SaPI1 procapsids to near-atomic resolution by cryo-electron microscopy, and show that CpmB competes with the 80α scaffolding protein (SP) for a binding site on the capsid protein (CP), and works by altering the angle between capsomers. We probed these interactions genetically and identified second-site suppressors of lethal mutations in SP. Our structures show, for the first time, the detailed interactions between SP and CP in a bacteriophage, providing unique insights into macromolecular assembly processes. eLife Sciences Publications, Ltd 2017-10-06 /pmc/articles/PMC5644958/ /pubmed/28984245 http://dx.doi.org/10.7554/eLife.30822 Text en © 2017, Dearborn et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Structural Biology and Molecular Biophysics Dearborn, Altaira D Wall, Erin A Kizziah, James L Klenow, Laura Parker, Laura K Manning, Keith A Spilman, Michael S Spear, John M Christie, Gail E Dokland, Terje Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title | Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title_full | Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title_fullStr | Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title_full_unstemmed | Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title_short | Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands |
title_sort | competing scaffolding proteins determine capsid size during mobilization of staphylococcus aureus pathogenicity islands |
topic | Structural Biology and Molecular Biophysics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5644958/ https://www.ncbi.nlm.nih.gov/pubmed/28984245 http://dx.doi.org/10.7554/eLife.30822 |
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