Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single particle cryo-electron microscopy (cryo-EM) yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6 Å and 9 Å resolution, respectively. The asymmetric reconstructi...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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Nature Publishing Group
2011
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| Online Access: | http://hdl.handle.net/1721.1/61294 https://orcid.org/0000-0003-1072-6828 |
| _version_ | 1811097350177816576 |
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| author | Liu, Xiangan Zhang, Qinfen Murata, Kazuyoshi Baker, Matthew L. Sullivan, Matthew B. Fu, Caroline Dougherty, Matthew Schmid, Michael F. Osburne, Marcia Chisholm, Sallie (Penny) Chiu, Wah |
| author2 | Massachusetts Institute of Technology. Department of Civil and Environmental Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Civil and Environmental Engineering Liu, Xiangan Zhang, Qinfen Murata, Kazuyoshi Baker, Matthew L. Sullivan, Matthew B. Fu, Caroline Dougherty, Matthew Schmid, Michael F. Osburne, Marcia Chisholm, Sallie (Penny) Chiu, Wah |
| author_sort | Liu, Xiangan |
| collection | MIT |
| description | Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic
photosynthetic microorganism. Single particle cryo-electron microscopy (cryo-EM) yields
icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6 Å and 9 Å resolution,
respectively. The asymmetric reconstruction reveals how symmetry mismatches are
accommodated among 5 of the gene products at the portal vertex. Reconstructions of
infectious and empty particles show a conformational change of the “valve” density in the
nozzle, an orientation difference in the tail fibers, a disordering of the C-terminus of the
portal protein, and disappearance of the core proteins. In addition, cryo-electron tomography
(cryo-ET) of P-SSP7 infecting Prochlorococcus demonstrated the same tail fiber conformation
as in empty particles. Our observations suggest a mechanism whereby, upon binding to the
host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release. |
| first_indexed | 2024-09-23T16:57:53Z |
| format | Article |
| id | mit-1721.1/61294 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T16:57:53Z |
| publishDate | 2011 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | mit-1721.1/612942022-10-03T09:28:21Z Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus Liu, Xiangan Zhang, Qinfen Murata, Kazuyoshi Baker, Matthew L. Sullivan, Matthew B. Fu, Caroline Dougherty, Matthew Schmid, Michael F. Osburne, Marcia Chisholm, Sallie (Penny) Chiu, Wah Massachusetts Institute of Technology. Department of Civil and Environmental Engineering Chisholm, Sallie (Penny) Sullivan, Matthew B. Osburne, Marcia Chisholm, Sallie (Penny) Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single particle cryo-electron microscopy (cryo-EM) yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6 Å and 9 Å resolution, respectively. The asymmetric reconstruction reveals how symmetry mismatches are accommodated among 5 of the gene products at the portal vertex. Reconstructions of infectious and empty particles show a conformational change of the “valve” density in the nozzle, an orientation difference in the tail fibers, a disordering of the C-terminus of the portal protein, and disappearance of the core proteins. In addition, cryo-electron tomography (cryo-ET) of P-SSP7 infecting Prochlorococcus demonstrated the same tail fiber conformation as in empty particles. Our observations suggest a mechanism whereby, upon binding to the host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release. National Institutes of Health (U.S) (P41RR002250) National Institutes of Health (U.S) (R01GM079429) National Science Foundation (U.S.) (IIS-0705644) Robert A. Welch Foundation (Q1242) United States. Dept. of Energy Gordon and Betty Moore Foundation 2011-02-23T14:51:07Z 2011-02-23T14:51:07Z 2010-06 2009-11 Article http://purl.org/eprint/type/JournalArticle 1545-9993 1545-9985 http://hdl.handle.net/1721.1/61294 Liu, Xiangan et al. “Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus.” Nat Struct Mol Biol 17.7 (2010): 830-836. https://orcid.org/0000-0003-1072-6828 en_US http://dx.doi.org/10.1038/nsmb.1823 Nature Structural and Molecular Biology Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Nature Publishing Group |
| spellingShingle | Liu, Xiangan Zhang, Qinfen Murata, Kazuyoshi Baker, Matthew L. Sullivan, Matthew B. Fu, Caroline Dougherty, Matthew Schmid, Michael F. Osburne, Marcia Chisholm, Sallie (Penny) Chiu, Wah Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title | Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title_full | Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title_fullStr | Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title_full_unstemmed | Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title_short | Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus |
| title_sort | structural changes in a marine podovirus associated with release of its genome into prochlorococcus |
| url | http://hdl.handle.net/1721.1/61294 https://orcid.org/0000-0003-1072-6828 |
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