scholarly journals The RNA binding protein Npl3 promotes resection of DNA double-strand breaks by regulating the levels of Exo1

2017 ◽  
Vol 45 (11) ◽  
pp. 6530-6545 ◽  
Author(s):  
Chiara Vittoria Colombo ◽  
Camilla Trovesi ◽  
Luca Menin ◽  
Maria Pia Longhese ◽  
Michela Clerici
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Strand Breaks

scholarly journals PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks

2012 ◽  
Vol 40 (20) ◽  
pp. 10287-10301 ◽  
Author(s):  
Jana Krietsch ◽  
Marie-Christine Caron ◽  
Jean-Philippe Gagné ◽  
Chantal Ethier ◽  
Julien Vignard ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Parp Activation ◽  
Strand Breaks ◽  
Damage Response

scholarly journals Detection of Endogenous DNA Double-strand Breaks in Oral Squamous Epithelial Lesions by P53-binding Protein 1

2021 ◽  
Vol 41 (10) ◽  
pp. 4771-4779
Author(s):  
TOSHINOBU IMAIZUMI ◽  
KATSUYA MATSUDA ◽  
KEI TANAKA ◽  
HISAYOSHI KONDO ◽  
NOZOMI UEKI ◽  
...  
Keyword(s):  
Binding Protein ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Strand Breaks ◽  
Epithelial Lesions

scholarly journals P53 Binding Protein 1 (53bp1) Is an Early Participant in the Cellular Response to DNA Double-Strand Breaks

2000 ◽  
Vol 151 (7) ◽  
pp. 1381-1390 ◽  
Author(s):  
Linda B. Schultz ◽  
Nabil H. Chehab ◽  
Asra Malikzay ◽  
Thanos D. Halazonetis
Keyword(s):  
Dna Damage ◽  
Cellular Response ◽  
Binding Protein ◽  
Intracellular Localization ◽  
Double Strand Breaks ◽  
Nuclear Staining ◽  
Dna Double Strand Breaks ◽  
Focus Formation ◽  
Fast Kinetics ◽  
Strand Breaks

p53 binding protein 1 (53BP1), a protein proposed to function as a transcriptional coactivator of the p53 tumor suppressor, has BRCT domains with high homology to the Saccharomyces cerevisiae Rad9p DNA damage checkpoint protein. To examine whether 53BP1 has a role in the cellular response to DNA damage, we probed its intracellular localization by immunofluorescence. In untreated primary cells and U2OS osteosarcoma cells, 53BP1 exhibited diffuse nuclear staining; whereas, within 5–15 min after exposure to ionizing radiation (IR), 53BP1 localized at discreet nuclear foci. We propose that these foci represent sites of processing of DNA double-strand breaks (DSBs), because they were induced by IR and chemicals that cause DSBs, but not by ultraviolet light; their peak number approximated the number of DSBs induced by IR and decreased over time with kinetics that parallel the rate of DNA repair; and they colocalized with IR-induced Mre11/NBS and γ-H2AX foci, which have been previously shown to localize at sites of DSBs. Formation of 53BP1 foci after irradiation was not dependent on ataxia-telangiectasia mutated (ATM), Nijmegen breakage syndrome (NBS1), or wild-type p53. Thus, the fast kinetics of 53BP1 focus formation after irradiation and the lack of dependency on ATM and NBS1 suggest that 53BP1 functions early in the cellular response to DNA DSBs.

scholarly journals Assembling nuclear domains: Lessons from DNA repair

2019 ◽  
Vol 218 (8) ◽  
pp. 2444-2455 ◽  
Author(s):  
Benjamin Schrank ◽  
Jean Gautier
Keyword(s):  
Rna Binding ◽  
Rna Binding Proteins ◽  
Low Complexity ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Strand Breaks ◽  
Dna Dsbs ◽  
Topologically Associated Domains ◽  
Nuclear Domains ◽  
Liquid Liquid Phase Separation

Eukaryotic nuclei are organized into nuclear domains that unite loci sharing a common function. These domains are essential for diverse processes including (1) the formation of topologically associated domains (TADs) that coordinate replication and transcription, (2) the formation of specialized transcription and splicing factories, and (3) the clustering of DNA double-strand breaks (DSBs), which concentrates damaged DNA for repair. The generation of nuclear domains requires forces that are beginning to be identified. In the case of DNA DSBs, DNA movement and clustering are driven by actin filament nucleators. Furthermore, RNAs and low-complexity protein domains such as RNA-binding proteins also accumulate around sites of transcription and repair. The link between liquid–liquid phase separation and actin nucleation in the formation of nuclear domains is still unknown. This review discusses DSB repair domain formation as a model for functional nuclear domains in other genomic contexts.

Repair pathway choice for double-strand breaks

2020 ◽  
Vol 64 (5) ◽  
pp. 765-777 ◽  
Author(s):  
Yixi Xu ◽  
Dongyi Xu
Keyword(s):  
Cell Cycle ◽  
Double Strand Breaks ◽  
Homologous Region ◽  
Gene Repair ◽  
Repair Pathway ◽  
Dna Double Strand Breaks ◽  
Environmental Radiation ◽  
Strand Breaks ◽  
Dna End Resection ◽  
End Resection

Abstract Deoxyribonucleic acid (DNA) is at a constant risk of damage from endogenous substances, environmental radiation, and chemical stressors. DNA double-strand breaks (DSBs) pose a significant threat to genomic integrity and cell survival. There are two major pathways for DSB repair: nonhomologous end-joining (NHEJ) and homologous recombination (HR). The extent of DNA end resection, which determines the length of the 3′ single-stranded DNA (ssDNA) overhang, is the primary factor that determines whether repair is carried out via NHEJ or HR. NHEJ, which does not require a 3′ ssDNA tail, occurs throughout the cell cycle. 53BP1 and the cofactors PTIP or RIF1-shieldin protect the broken DNA end, inhibit long-range end resection and thus promote NHEJ. In contrast, HR mainly occurs during the S/G2 phase and requires DNA end processing to create a 3′ tail that can invade a homologous region, ensuring faithful gene repair. BRCA1 and the cofactors CtIP, EXO1, BLM/DNA2, and the MRE11–RAD50–NBS1 (MRN) complex promote DNA end resection and thus HR. DNA resection is influenced by the cell cycle, the chromatin environment, and the complexity of the DNA end break. Herein, we summarize the key factors involved in repair pathway selection for DSBs and discuss recent related publications.

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