TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts
Eukaryotic topoisomerase 1 (TOP1) regulates DNA topology to ensure efficient DNA replication and transcription. Here, the authors reveal insights into the molecular resolution of topoisomerase 1-DNA adducts by TEX264, p97 and SPRTN.
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2020-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-15000-w |
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doaj-8eb6f2f6a3d047b7b8052b86b27f77252021-05-11T09:07:11ZengNature Publishing GroupNature Communications2041-17232020-03-0111111610.1038/s41467-020-15000-wTEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adductsJohn Fielden0Katherine Wiseman1Ignacio Torrecilla2Shudong Li3Samuel Hume4Shih-Chieh Chiang5Annamaria Ruggiano6Abhay Narayan Singh7Raimundo Freire8Sylvana Hassanieh9Enric Domingo10Iolanda Vendrell11Roman Fischer12Benedikt M. Kessler13Timothy S. Maughan14Sherif F. El-Khamisy15Kristijan Ramadan16Cancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordThe University of Sheffield Neuroscience Institute and the Healthy Lifespan Institute, Department of Molecular Biology and Biotechnology, Firth Court, University of SheffieldCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordUnidad de Investigación, Hospital Universitario de Canarias, Ofra s/n, La CuestaCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordTDI Mass Spectrometry Laboratory, Target Discovery Institute, Nuffield Department of Medicine, University of OxfordTDI Mass Spectrometry Laboratory, Target Discovery Institute, Nuffield Department of Medicine, University of OxfordCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordThe University of Sheffield Neuroscience Institute and the Healthy Lifespan Institute, Department of Molecular Biology and Biotechnology, Firth Court, University of SheffieldCancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of OxfordEukaryotic topoisomerase 1 (TOP1) regulates DNA topology to ensure efficient DNA replication and transcription. Here, the authors reveal insights into the molecular resolution of topoisomerase 1-DNA adducts by TEX264, p97 and SPRTN.https://doi.org/10.1038/s41467-020-15000-w |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
John Fielden Katherine Wiseman Ignacio Torrecilla Shudong Li Samuel Hume Shih-Chieh Chiang Annamaria Ruggiano Abhay Narayan Singh Raimundo Freire Sylvana Hassanieh Enric Domingo Iolanda Vendrell Roman Fischer Benedikt M. Kessler Timothy S. Maughan Sherif F. El-Khamisy Kristijan Ramadan |
| spellingShingle |
John Fielden Katherine Wiseman Ignacio Torrecilla Shudong Li Samuel Hume Shih-Chieh Chiang Annamaria Ruggiano Abhay Narayan Singh Raimundo Freire Sylvana Hassanieh Enric Domingo Iolanda Vendrell Roman Fischer Benedikt M. Kessler Timothy S. Maughan Sherif F. El-Khamisy Kristijan Ramadan TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts Nature Communications |
| author_facet |
John Fielden Katherine Wiseman Ignacio Torrecilla Shudong Li Samuel Hume Shih-Chieh Chiang Annamaria Ruggiano Abhay Narayan Singh Raimundo Freire Sylvana Hassanieh Enric Domingo Iolanda Vendrell Roman Fischer Benedikt M. Kessler Timothy S. Maughan Sherif F. El-Khamisy Kristijan Ramadan |
| author_sort |
John Fielden |
| title |
TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts |
| title_short |
TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts |
| title_full |
TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts |
| title_fullStr |
TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts |
| title_full_unstemmed |
TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts |
| title_sort |
tex264 coordinates p97- and sprtn-mediated resolution of topoisomerase 1-dna adducts |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2020-03-01 |
| description |
Eukaryotic topoisomerase 1 (TOP1) regulates DNA topology to ensure efficient DNA replication and transcription. Here, the authors reveal insights into the molecular resolution of topoisomerase 1-DNA adducts by TEX264, p97 and SPRTN. |
| url |
https://doi.org/10.1038/s41467-020-15000-w |
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