Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer
Retroviral integrases catalyze the insertion of viral DNA into the host cell DNA and can use nucleosomes as substrates for integration. Here the authors present the 3.9 Å cryo-EM structure of prototype foamy virus integrase after strand transfer into nucleosomal DNA, which together with single-molec...
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2019-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-12007-w |
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Article |
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doaj-81003a4887374f70b3a53f31395ad7bb2021-05-11T12:38:27ZengNature Publishing GroupNature Communications2041-17232019-09-0110111010.1038/s41467-019-12007-wRetroviral integration into nucleosomes through DNA looping and sliding along the histone octamerMarcus D. Wilson0Ludovic Renault1Daniel P. Maskell2Mohamed Ghoneim3Valerie E. Pye4Andrea Nans5David S. Rueda6Peter Cherepanov7Alessandro Costa8Macromolecular Machines Laboratory, The Francis Crick InstituteMacromolecular Machines Laboratory, The Francis Crick InstituteChromatin structure and mobile DNA Laboratory, The Francis Crick InstituteSingle Molecule Imaging Group, MRC London Institute for Medical ScienceChromatin structure and mobile DNA Laboratory, The Francis Crick InstituteStructural Biology Science Technology Platform, The Francis Crick InstituteSingle Molecule Imaging Group, MRC London Institute for Medical ScienceChromatin structure and mobile DNA Laboratory, The Francis Crick InstituteMacromolecular Machines Laboratory, The Francis Crick InstituteRetroviral integrases catalyze the insertion of viral DNA into the host cell DNA and can use nucleosomes as substrates for integration. Here the authors present the 3.9 Å cryo-EM structure of prototype foamy virus integrase after strand transfer into nucleosomal DNA, which together with single-molecule FRET measurements provides evidence for a DNA looping and sliding mechanism of integrases.https://doi.org/10.1038/s41467-019-12007-w |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Marcus D. Wilson Ludovic Renault Daniel P. Maskell Mohamed Ghoneim Valerie E. Pye Andrea Nans David S. Rueda Peter Cherepanov Alessandro Costa |
| spellingShingle |
Marcus D. Wilson Ludovic Renault Daniel P. Maskell Mohamed Ghoneim Valerie E. Pye Andrea Nans David S. Rueda Peter Cherepanov Alessandro Costa Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer Nature Communications |
| author_facet |
Marcus D. Wilson Ludovic Renault Daniel P. Maskell Mohamed Ghoneim Valerie E. Pye Andrea Nans David S. Rueda Peter Cherepanov Alessandro Costa |
| author_sort |
Marcus D. Wilson |
| title |
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer |
| title_short |
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer |
| title_full |
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer |
| title_fullStr |
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer |
| title_full_unstemmed |
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer |
| title_sort |
retroviral integration into nucleosomes through dna looping and sliding along the histone octamer |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2019-09-01 |
| description |
Retroviral integrases catalyze the insertion of viral DNA into the host cell DNA and can use nucleosomes as substrates for integration. Here the authors present the 3.9 Å cryo-EM structure of prototype foamy virus integrase after strand transfer into nucleosomal DNA, which together with single-molecule FRET measurements provides evidence for a DNA looping and sliding mechanism of integrases. |
| url |
https://doi.org/10.1038/s41467-019-12007-w |
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