scholarly journals Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus

2021 ◽  
pp. 100921
Author(s):  
Ishtiaque Rashid ◽  
Michal Hammel ◽  
Aleksandr Sverzhinsky ◽  
Miaw-Sheue Tsai ◽  
John M. Pascal ◽  
...  
Keyword(s):  
Dna Repair ◽  
Catalytic Domain ◽  
Direct Interaction ◽  
Dna Ligase ◽  
Repair Protein ◽  
N Terminus ◽  
Dna Repair Protein ◽  
Dna Ligase Iii

scholarly journals Role of a BRCT domain in the interaction of DNA ligase III-α with the DNA repair protein XRCC1

1998 ◽  
Vol 8 (15) ◽  
pp. 877-880 ◽  
Author(s):  
Richard M. Taylor ◽  
Bill Wickstead ◽  
Sam Cronin ◽  
Keith W. Caldecott
Keyword(s):  
Dna Repair ◽  
Dna Ligase ◽  
Brct Domain ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Dna Ligase Iii

BRCT Domain Interactions in the Heterodimeric DNA Repair Protein XRCC1−DNA Ligase III†

Biochemistry ◽  
2001 ◽  
Vol 40 (20) ◽  
pp. 5906-5913 ◽  
Author(s):  
Anna Dulic ◽  
Paul A. Bates ◽  
Xiaodong Zhang ◽  
Stephen R. Martin ◽  
Paul S. Freemont ◽  
...  
Keyword(s):  
Dna Repair ◽  
Dna Ligase ◽  
Brct Domain ◽  
Repair Protein ◽  
Domain Interactions ◽  
Dna Repair Protein ◽  
Dna Ligase Iii

The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23

2004 ◽  
Vol 323 (1) ◽  
pp. 149-155 ◽  
Author(s):  
Shyamasri Biswas ◽  
Samiksha Katiyar ◽  
Guangtao Li ◽  
Xiaoke Zhou ◽  
William J. Lennarz ◽  
...  
Keyword(s):  
Dna Repair ◽  
Repair Protein ◽  
N Terminus ◽  
Dna Repair Protein

scholarly journals A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M

2005 ◽  
Vol 37 (9) ◽  
pp. 958-963 ◽  
Author(s):  
Amom Ruhikanta Meetei ◽  
Annette L Medhurst ◽  
Chen Ling ◽  
Yutong Xue ◽  
Thiyam Ramsing Singh ◽  
...  
Keyword(s):  
Dna Repair ◽  
Fanconi Anemia ◽  
Complementation Group ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Human Ortholog

Chemoproteomics-Enabled Discovery of a Potent and Selective Inhibitor of the DNA Repair Protein MGMT

2016 ◽  
Vol 55 (8) ◽  
pp. 2911-2915 ◽  
Author(s):  
Chao Wang ◽  
Daniel Abegg ◽  
Dominic G. Hoch ◽  
Alexander Adibekian
Keyword(s):  
Dna Repair ◽  
Selective Inhibitor ◽  
Repair Protein ◽  
Dna Repair Protein

scholarly journals An interaction between the mammalian DNA repair protein XRCC1 and DNA ligase III.

1994 ◽  
Vol 14 (1) ◽  
pp. 68-76 ◽  
Author(s):  
K W Caldecott ◽  
C K McKeown ◽  
J D Tucker ◽  
S Ljungquist ◽  
L H Thompson
Keyword(s):  
Dna Repair ◽  
Affinity Chromatography ◽  
Mammalian Cells ◽  
Excision Repair ◽  
Affinity Purification ◽  
Alkylating Agents ◽  
Chinese Hamster ◽  
Dna Ligase ◽  
Base Excision ◽  
Dna Ligase Iii

XRCC1, the human gene that fully corrects the Chinese hamster ovary DNA repair mutant EM9, encodes a protein involved in the rejoining of DNA single-strand breaks that arise following treatment with alkylating agents or ionizing radiation. In this study, a cDNA minigene encoding oligohistidine-tagged XRCC1 was constructed to facilitate affinity purification of the recombinant protein. This construct, designated pcD2EHX, fully corrected the EM9 phenotype of high sister chromatid exchange, indicating that the histidine tag was not detrimental to XRCC1 activity. Affinity chromatography of extract from EM9 cells transfected with pcD2EHX resulted in the copurification of histidine-tagged XRCC1 and DNA ligase III activity. Neither XRCC1 or DNA ligase III activity was purified during affinity chromatography of extract from EM9 cells transfected with pcD2EX, a cDNA minigene that encodes untagged XRCC1, or extract from wild-type AA8 or untransfected EM9 cells. The copurification of DNA ligase III activity with histidine-tagged XRCC1 suggests that the two proteins are present in the cell as a complex. Furthermore, DNA ligase III activity was present at lower levels in EM9 cells than in AA8 cells and was returned to normal levels in EM9 cells transfected with pcD2EHX or pcD2EX. These findings indicate that XRCC1 is required for normal levels of DNA ligase III activity, and they implicate a major role for this DNA ligase in DNA base excision repair in mammalian cells.

Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

1995 ◽  
Vol 337 (1) ◽  
pp. 25-39 ◽  
Author(s):  
A.J. van Vuuren ◽  
E. Appeldoorn ◽  
H. Odijk ◽  
S. Humbert ◽  
V. Moncollin ◽  
...  
Keyword(s):  
Dna Repair ◽  
Protein Complex ◽  
Partial Characterization ◽  
Repair Protein ◽  
Dna Repair Protein

scholarly journals ROS induces NETosis by oxidizing DNA and initiating DNA repair

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Dhia Azzouz ◽  
Meraj A. Khan ◽  
Nades Palaniyar
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Polymerase Activity ◽  
Neutrophil Activation ◽  
Neutrophil Extracellular Trap ◽  
Nuclear Antigen ◽  
Chromatin Decondensation ◽  
Genome Wide ◽  
Repair Protein ◽  
Dna Repair Protein

AbstractReactive oxygen species (ROS) are essential for neutrophil extracellular trap (NET) formation or NETosis. Nevertheless, how ROS induces NETosis is unknown. Neutrophil activation induces excess ROS production and a meaningless genome-wide transcription to facilitate chromatin decondensation. Here we show that the induction of NADPH oxidase-dependent NETosis leads to extensive DNA damage, and the subsequent translocation of proliferating cell nuclear antigen (PCNA), a key DNA repair protein, stored in the cytoplasm into the nucleus. During the activation of NETosis (e.g., by phorbol myristate acetate, Escherichia coli LPS, Staphylococcus aureus (RN4220), or Pseudomonas aeruginosa), preventing the DNA-repair-complex assembly leading to nick formation that decondenses chromatin causes the suppression of NETosis (e.g., by inhibitors to, or knockdown of, Apurinic endonuclease APE1, poly ADP ribose polymerase PARP, and DNA ligase). The remaining repair steps involving polymerase activity and PCNA interactions with DNA polymerases β/δ do not suppress agonist-induced NETosis. Therefore, excess ROS produced during neutrophil activation induces NETosis by inducing extensive DNA damage (e.g., oxidising guanine to 8-oxoguanine), and the subsequent DNA repair pathway, leading to chromatin decondensation.

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