Regulation of DNA End Joining, Resection, and Immunoglobulin Class Switch Recombination by 53BP1
Open accessAbstract
53BP1 is a DNA damage protein that forms phosphorylated H2AX (γ-H2AX) dependent foci in a 1 Mb region surrounding DNA double-strand breaks (DSBs). In addition, 53BP1 promotes genomic stability by regulating the metabolism of DNA ends. We have compared the joining rates of paired DSBs separated by 1.2 kb to 27 Mb on chromosome 12 in the presence or absence of 53BP1. 53BP1 facilitates joining of intrachromosomal DSBs but only at distances corresponding to γ-H2AX spreading. In contrast, DNA end protection by 53BP1 is distance independent. Furthermore, analysis of 53BP1 mutants shows that chromatin association, oligomerization, and N-terminal ATM phosphorylation are all required for DNA end protection and joining as measured by immunoglobulin class switch recombination. These data elucidate the molecular events that are required for 53BP1 to maintain genomic stability and point to a model wherein 53BP1 and H2AX cooperate to repress resection of DSBs.
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The fraction of alleles that underwent DSB formation and repair is expected to be significantly greater than 33%, because proximal DSB ends join more efficiently than distant ones.
“Given that the joining of proximal DSB ends is considerably more efficient than that of more distant ones (41), we expect the fraction of alleles that have undergone DSB formation and repair to be significantly greater than 33%.”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [41]
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- Authors
- Bothmer, A., Robbiani, D. F., Di Virgilio, M., Bunting, S. F., Klein, I. A., Feldhahn, N., Barlow, J., Chen, H.-T., Bosque, D., Callen, E., Nussenzweig, A., & Nussenzweig, M. C.
- Affiliations
- Rockefeller University (US)
- National Institutes of Health (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nussenzweig, André
- Nussenzweig, Michel C.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-05
- Volume
- 42
- Issue
- 3
- Pages
- 319-329
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3142663
- OpenAlex
- W2052981964
- Cited by
- 244
- References
- 55
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 7 · 2023: 8 · 2022: 12 · 2021: 13 · 2020: 13 · 2019: 16 · 2018: 9 · 2017: 13 · 2016: 17 · 2015: 22 · 2014: 25 · 2013: 45 · 2012: 23
- FWCI
- 12.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Institute of General Medical Sciences (GM 07739, T32GM007739)
- National Institute of Allergy and Infectious Diseases (R37AI037526, R01AI037526, R01AI072529, AI037526)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- 53BP1, DNA double-strand break repair, DNA end joining, DNA end resection, immunoglobulin class switch recombination, γH2AX, ATM phosphorylation, genome stability, DNA end protection, chromatin association, oligomerization, chromosome 12
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, Animals, B-Lymphocytes, Binding Sites, Cells, Cultured, Chromatin, Chromosomal Proteins, Non-Histone, DNA Repair, DNA-Binding Proteins, Flow Cytometry, Histones, Mice, Inbred C57BL, Models, Genetic, Phosphorylation, Recombination, Genetic, Blotting, Western, Immunoglobulin Class Switching, Mice, Knockout, Mice, DNA Breaks, Double-Stranded, Protein Multimerization
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