DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner

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

doi:10.1038/s41467-020-16926-x

Nature Communications (Jun 2020)

DNA double-strand breaks induce H2Ax phosphorylation domains in a contact-dependent manner

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

Affiliations

Patrick L. Collins: Department of Microbial Infection and Immunity, The Ohio State University
Caitlin Purman: Department of Pathology and Immunology, Washington University School of Medicine
Sofia I. Porter: Department of Microbial Infection and Immunity, The Ohio State University
Vincent Nganga: Department of Microbial Infection and Immunity, The Ohio State University
Ankita Saini: Department of Microbial Infection and Immunity, The Ohio State University
Katharina E. Hayer: Department of Biomedical and Health Informatics, Children’s Hospital of Philadelphia
Greer L. Gurewitz: Department of Pathology and Immunology, Washington University School of Medicine
Barry P. Sleckman: Department of Medicine, Division of Hematology and Oncology, O’Neal Comprehensive Cancer Center, University of Alabama at Birmingham
Jeffrey J. Bednarski: Department of Pediatrics, Washington University School of Medicine
Craig H. Bassing: Department of Pathology and Laboratory Medicine, Children’s Hospital of Philadelphia, Perelman School of Medicine, University of Pennsylvania
Eugene M. Oltz: Department of Microbial Infection and Immunity, The Ohio State University

DOI: https://doi.org/10.1038/s41467-020-16926-x
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 9

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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