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Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Proceedings of the National Academy of Sciences, 115, 2018, 19, S. 4992-4997 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
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Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell |
|---|---|
| author |
Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell |
| spellingShingle |
Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell Proceedings of the National Academy of Sciences Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether Multidisciplinary |
| author_sort |
grant, margaret j. |
| spelling |
Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1721638115 <jats:title>Significance</jats:title> <jats:p>Kaposi’s sarcoma-associated herpesvirus propagates by attaching to host chromatin. This tether is essential for viral maintenance, and its disruption represents a potential treatment for persistent infection. However, fundamental questions remain, including how the underlying viral chromatin is folded, how the tether protein is organized, and how it is presented for host attachment. Using superresolution fluorescence microscopy, we have visualized single tethers in cells and built a working model of their structure. The folding of the viral chromatin mimics that of active chromatin, driven by nucleosome positioning and DNA bending. Furthermore, tether proteins are arranged in ordered clusters projected outward from the viral chromatin axis. These principles are likely to be applicable to the tethers of other DNA tumor viruses.</jats:p> Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether Proceedings of the National Academy of Sciences |
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| title |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_unstemmed |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_full |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_fullStr |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_full_unstemmed |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_short |
Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_sort |
superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
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Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.1721638115 |
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2018 |
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4992-4997 |
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<jats:title>Significance</jats:title>
<jats:p>Kaposi’s sarcoma-associated herpesvirus propagates by attaching to host chromatin. This tether is essential for viral maintenance, and its disruption represents a potential treatment for persistent infection. However, fundamental questions remain, including how the underlying viral chromatin is folded, how the tether protein is organized, and how it is presented for host attachment. Using superresolution fluorescence microscopy, we have visualized single tethers in cells and built a working model of their structure. The folding of the viral chromatin mimics that of active chromatin, driven by nucleosome positioning and DNA bending. Furthermore, tether proteins are arranged in ordered clusters projected outward from the viral chromatin axis. These principles are likely to be applicable to the tethers of other DNA tumor viruses.</jats:p> |
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| author | Grant, Margaret J., Loftus, Matthew S., Stoja, Aiola P., Kedes, Dean H., Smith, M. Mitchell |
| author_facet | Grant, Margaret J., Loftus, Matthew S., Stoja, Aiola P., Kedes, Dean H., Smith, M. Mitchell, Grant, Margaret J., Loftus, Matthew S., Stoja, Aiola P., Kedes, Dean H., Smith, M. Mitchell |
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| description | <jats:title>Significance</jats:title> <jats:p>Kaposi’s sarcoma-associated herpesvirus propagates by attaching to host chromatin. This tether is essential for viral maintenance, and its disruption represents a potential treatment for persistent infection. However, fundamental questions remain, including how the underlying viral chromatin is folded, how the tether protein is organized, and how it is presented for host attachment. Using superresolution fluorescence microscopy, we have visualized single tethers in cells and built a working model of their structure. The folding of the viral chromatin mimics that of active chromatin, driven by nucleosome positioning and DNA bending. Furthermore, tether proteins are arranged in ordered clusters projected outward from the viral chromatin axis. These principles are likely to be applicable to the tethers of other DNA tumor viruses.</jats:p> |
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| spelling | Grant, Margaret J. Loftus, Matthew S. Stoja, Aiola P. Kedes, Dean H. Smith, M. Mitchell 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1721638115 <jats:title>Significance</jats:title> <jats:p>Kaposi’s sarcoma-associated herpesvirus propagates by attaching to host chromatin. This tether is essential for viral maintenance, and its disruption represents a potential treatment for persistent infection. However, fundamental questions remain, including how the underlying viral chromatin is folded, how the tether protein is organized, and how it is presented for host attachment. Using superresolution fluorescence microscopy, we have visualized single tethers in cells and built a working model of their structure. The folding of the viral chromatin mimics that of active chromatin, driven by nucleosome positioning and DNA bending. Furthermore, tether proteins are arranged in ordered clusters projected outward from the viral chromatin axis. These principles are likely to be applicable to the tethers of other DNA tumor viruses.</jats:p> Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether Proceedings of the National Academy of Sciences |
| spellingShingle | Grant, Margaret J., Loftus, Matthew S., Stoja, Aiola P., Kedes, Dean H., Smith, M. Mitchell, Proceedings of the National Academy of Sciences, Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether, Multidisciplinary |
| title | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_full | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_fullStr | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_full_unstemmed | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_short | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_sort | superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| title_unstemmed | Superresolution microscopy reveals structural mechanisms driving the nanoarchitecture of a viral chromatin tether |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1721638115 |