DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner
Formation of γH2Ax serves as a checkpoint for double-strand break (DSB) repair pathways. Here the authors reveal via integrated chromatin analysis that γH2Ax domains are established by chromosomal contacts with the DSB site.
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2020-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-16926-x |
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doaj-52e96531818443018246302cc0d348bc |
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Article |
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doaj-52e96531818443018246302cc0d348bc2021-06-27T11:14:47ZengNature Publishing GroupNature Communications2041-17232020-06-011111910.1038/s41467-020-16926-xDNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent mannerPatrick L. Collins0Caitlin Purman1Sofia I. Porter2Vincent Nganga3Ankita Saini4Katharina E. Hayer5Greer L. Gurewitz6Barry P. Sleckman7Jeffrey J. Bednarski8Craig H. Bassing9Eugene M. Oltz10Department of Microbial Infection and Immunity, The Ohio State UniversityDepartment of Pathology and Immunology, Washington University School of MedicineDepartment of Microbial Infection and Immunity, The Ohio State UniversityDepartment of Microbial Infection and Immunity, The Ohio State UniversityDepartment of Microbial Infection and Immunity, The Ohio State UniversityDepartment of Biomedical and Health Informatics, Children’s Hospital of PhiladelphiaDepartment of Pathology and Immunology, Washington University School of MedicineDepartment of Medicine, Division of Hematology and Oncology, O’Neal Comprehensive Cancer Center, University of Alabama at BirminghamDepartment of Pediatrics, Washington University School of MedicineDepartment of Pathology and Laboratory Medicine, Children’s Hospital of Philadelphia, Perelman School of Medicine, University of PennsylvaniaDepartment of Microbial Infection and Immunity, The Ohio State UniversityFormation of γH2Ax serves as a checkpoint for double-strand break (DSB) repair pathways. Here the authors reveal via integrated chromatin analysis that γH2Ax domains are established by chromosomal contacts with the DSB site.https://doi.org/10.1038/s41467-020-16926-x |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Patrick L. Collins Caitlin Purman Sofia I. Porter Vincent Nganga Ankita Saini Katharina E. Hayer Greer L. Gurewitz Barry P. Sleckman Jeffrey J. Bednarski Craig H. Bassing Eugene M. Oltz |
| spellingShingle |
Patrick L. Collins Caitlin Purman Sofia I. Porter Vincent Nganga Ankita Saini Katharina E. Hayer Greer L. Gurewitz Barry P. Sleckman Jeffrey J. Bednarski Craig H. Bassing Eugene M. Oltz DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner Nature Communications |
| author_facet |
Patrick L. Collins Caitlin Purman Sofia I. Porter Vincent Nganga Ankita Saini Katharina E. Hayer Greer L. Gurewitz Barry P. Sleckman Jeffrey J. Bednarski Craig H. Bassing Eugene M. Oltz |
| author_sort |
Patrick L. Collins |
| title |
DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner |
| title_short |
DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner |
| title_full |
DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner |
| title_fullStr |
DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner |
| title_full_unstemmed |
DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner |
| title_sort |
dna double-strand breaks induce h2ax phosphorylation domains in a contact-dependent manner |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2020-06-01 |
| description |
Formation of γH2Ax serves as a checkpoint for double-strand break (DSB) repair pathways. Here the authors reveal via integrated chromatin analysis that γH2Ax domains are established by chromosomal contacts with the DSB site. |
| url |
https://doi.org/10.1038/s41467-020-16926-x |
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