scholarly journals A Chemical Genetics Analysis of the Roles of Bypass Polymerase DinB and DNA Repair Protein AlkB in Processing N2-Alkylguanine Lesions In Vivo

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94716 ◽  
Author(s):  
Nidhi Shrivastav ◽  
Bogdan I. Fedeles ◽  
Deyu Li ◽  
James C. Delaney ◽  
Lauren E. Frick ◽  
...  
Keyword(s):  
Dna Repair ◽  
Chemical Genetics ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Bypass Polymerase

scholarly journals Involvement of the DNA Repair Protein hHR23 inp53Degradation

2003 ◽  
Vol 23 (24) ◽  
pp. 8960-8969 ◽  
Author(s):  
Sandra Glockzin ◽  
Francois-Xavier Ogi ◽  
Arnd Hengstermann ◽  
Martin Scheffner ◽  
Christine Blattner
Keyword(s):  
Dna Repair ◽  
26S Proteasome ◽  
Polyubiquitin Chains ◽  
Proteolytic Pathway ◽  
Repair Protein ◽  
Uba Domain ◽  
Dna Repair Protein ◽  
The Stability

ABSTRACT The stability of the tumor suppressor protein p53 is regulated via the ubiquitin-proteasome-dependent proteolytic pathway. Like most substrates of this pathway, p53 is modified by the attachment of polyubiquitin chains prior to proteasome-mediated degradation. However, the mechanism(s) involved in the delivery of polyubiquitylated p53 molecules to the proteasome are currently unclear. Here, we show that the human DNA repair protein hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation in vitro and in vivo. In addition, downregulation of hHR23 expression within cells by RNA interference results in accumulation of p53. Since the Ubl domain of hHR23 has been shown to interact with the 26S proteasome, we propose that hHR23 is intrinsically involved in the delivery of polyubiquitylated p53 molecules to the proteasome. In this model, the Uba domain of hHR23 binds to polyubiquitin chains formed on p53 and protects them from deubiquitylation, while the Ubl domain delivers the polyubiquitylated p53 molecules to the proteasome.

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

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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