scholarly journals Sensitizing Ewing sarcoma to chemo- and radiotherapy by inhibition of the DNA-repair enzymes DNA protein kinase (DNA-PK) and poly-ADP-ribose polymerase (PARP) 1/2

Oncotarget ◽  
2017 ◽  
Vol 8 (69) ◽  
pp. 113418-113430 ◽  
Author(s):  
Britta Vormoor ◽  
Yvonne T. Schlosser ◽  
Helen Blair ◽  
Abhishek Sharma ◽  
Sarah Wilkinson ◽  
...  
Keyword(s):  
Dna Repair ◽  
Protein Kinase ◽  
Ewing Sarcoma ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Parp 1

scholarly journals Identification of Novel Interaction Partners of Ets-1: Focus on DNA Repair

Genes ◽  
2019 ◽  
Vol 10 (3) ◽  
pp. 206
Author(s):  
Guillaume Brysbaert ◽  
Jérôme de Ruyck ◽  
Marc Aumercier ◽  
Marc F. Lensink
Keyword(s):  
Dna Repair ◽  
Interaction Model ◽  
Protein Docking ◽  
Dna Repair Enzymes ◽  
Dna Repair Mechanisms ◽  
Repair Enzymes ◽  
Repair Mechanisms ◽  
Important Regulator ◽  
Dependent Protein ◽  
Parp 1

The transcription factor Ets-1 (ETS proto-oncogene 1) shows low expression levels except in specific biological processes like haematopoiesis or angiogenesis. Elevated levels of expression are observed in tumor progression, resulting in Ets-1 being named an oncoprotein. It has recently been shown that Ets-1 interacts with two DNA repair enzymes, PARP-1 (poly(ADP-ribose) polymerase 1) and DNA-PK (DNA-dependent protein kinase), through two different domains and that these interactions play a role in cancer. Considering that Ets-1 can bind to distinctly different domains of two DNA repair enzymes, we hypothesized that the interaction can be transposed onto homologs of the respective domains. We have searched for sequence and structure homologs of the interacting ETS(Ets-1), BRCT(PARP-1) and SAP(DNA-PK) domains, and have identified several candidate binding pairs that are currently not annotated as such. Many of the Ets-1 partners are associated to DNA repair mechanisms. We have applied protein-protein docking to establish putative interaction poses and investigated these using centrality analyses at the protein residue level. Most of the identified poses are virtually similar to our recently established interaction model for Ets-1/PARP-1 and Ets-1/DNA-PK. Our work illustrates the potentially high number of interactors of Ets-1, in particular involved in DNA repair mechanisms, which shows the oncoprotein as a potential important regulator of the mechanism.

scholarly journals Coordinated signals from the DNA repair enzymes PARP-1 and PARP-2 promotes B-cell development and function

2019 ◽  
Vol 26 (12) ◽  
pp. 2667-2681 ◽  
Author(s):  
Miguel A. Galindo-Campos ◽  
Marie Bedora-Faure ◽  
Jordi Farrés ◽  
Chloé Lescale ◽  
Lucia Moreno-Lama ◽  
...  
Keyword(s):  
Dna Repair ◽  
B Cell ◽  
Cell Development ◽  
B Cell Development ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
And Function ◽  
Parp 1

scholarly journals DASH-type cryptochromes – solved and open questions

2020 ◽  
Vol 401 (12) ◽  
pp. 1487-1493
Author(s):  
Stephan Kiontke ◽  
Tanja Göbel ◽  
Annika Brych ◽  
Alfred Batschauer
Keyword(s):  
Dna Repair ◽  
Circadian Clock ◽  
Blue Light ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Open Questions ◽  
Essential Components ◽  
Repair Activity ◽  
Almost All ◽  
Uv Lesions

AbstractDrosophila, Arabidopsis, Synechocystis, human (DASH)-type cryptochromes (cry-DASHs) form one subclade of the cryptochrome/photolyase family (CPF). CPF members are flavoproteins that act as DNA-repair enzymes (DNA-photolyases), or as ultraviolet(UV)-A/blue light photoreceptors (cryptochromes). In mammals, cryptochromes are essential components of the circadian clock feed-back loop. Cry-DASHs are present in almost all major taxa and were initially considered as photoreceptors. Later studies demonstrated DNA-repair activity that was, however, restricted to UV-lesions in single-stranded DNA. Very recent studies, particularly on microbial organisms, substantiated photoreceptor functions of cry-DASHs suggesting that they could be transitions between photolyases and cryptochromes.

DNA Repair Enzymes in Mammalian Cells

1977 ◽  
pp. 263-322 ◽  
Author(s):  
Errol C. Friedberg ◽  
Kern H. Cook ◽  
James Duncan ◽  
Kristien Mortelmans
Keyword(s):  
Dna Repair ◽  
Mammalian Cells ◽  
Dna Repair Enzymes ◽  
Repair Enzymes

scholarly journals DNA damage shifts circadian clock time via Hausp-dependent Cry1 stabilization

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Stephanie J Papp ◽  
Anne-Laure Huber ◽  
Sabine D Jordan ◽  
Anna Kriebs ◽  
Madelena Nguyen ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Circadian Clock ◽  
Transcriptional Response ◽  
Genotoxic Stress ◽  
Genomic Integrity ◽  
Clock Time ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Specific Protease

The circadian transcriptional repressors cryptochrome 1 (Cry1) and 2 (Cry2) evolved from photolyases, bacterial light-activated DNA repair enzymes. In this study, we report that while they have lost DNA repair activity, Cry1/2 adapted to protect genomic integrity by responding to DNA damage through posttranslational modification and coordinating the downstream transcriptional response. We demonstrate that genotoxic stress stimulates Cry1 phosphorylation and its deubiquitination by Herpes virus associated ubiquitin-specific protease (Hausp, a.k.a Usp7), stabilizing Cry1 and shifting circadian clock time. DNA damage also increases Cry2 interaction with Fbxl3, destabilizing Cry2. Thus, genotoxic stress increases the Cry1/Cry2 ratio, suggesting distinct functions for Cry1 and Cry2 following DNA damage. Indeed, the transcriptional response to genotoxic stress is enhanced in Cry1−/− and blunted in Cry2−/− cells. Furthermore, Cry2−/− cells accumulate damaged DNA. These results suggest that Cry1 and Cry2, which evolved from DNA repair enzymes, protect genomic integrity via coordinated transcriptional regulation.

scholarly journals Structural and cellular analyses of cancer-associated mutations in DNA repair enzymes

2019 ◽  
Vol 75 (a1) ◽  
pp. a327-a327
Author(s):  
Brian E. Eckenroth ◽  
Ash Prakash ◽  
Brittany L. Carroll ◽  
Joann B. Sweasy ◽  
Sylvie Doublié
Keyword(s):  
Dna Repair ◽  
Dna Repair Enzymes ◽  
Repair Enzymes
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