scholarly journals The retinoblastoma homolog RBR 1 mediates localization of the repair protein RAD 51 to DNA lesions in Arabidopsis

2017 ◽  
Vol 36 (9) ◽  
pp. 1279-1297 ◽  
Author(s):  
Sascha Biedermann ◽  
Hirofumi Harashima ◽  
Poyu Chen ◽  
Maren Heese ◽  
Daniel Bouyer ◽  
...  
Keyword(s):  
Dna Lesions ◽  
Repair Protein

scholarly journals Repair protein persistence at DNA lesions characterizes XPF defect with Cockayne syndrome features

2018 ◽  
Vol 46 (18) ◽  
pp. 9563-9577 ◽  
Author(s):  
Mariangela Sabatella ◽  
Arjan F Theil ◽  
Cristina Ribeiro-Silva ◽  
Jana Slyskova ◽  
Karen Thijssen ◽  
...  
Keyword(s):  
Cockayne Syndrome ◽  
Dna Lesions ◽  
Repair Protein

Distinct kinetics of DNA repair protein accumulation at DNA lesions and cell cycle-dependent formation of γH2AX- and NBS1-positive repair foci

2015 ◽  
Vol 107 (12) ◽  
pp. 440-454 ◽  
Author(s):  
Jana Suchánková ◽  
Stanislav Kozubek ◽  
Soňa Legartová ◽  
Petra Sehnalová ◽  
Thomas Küntziger ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Repair ◽  
Dna Lesions ◽  
Protein Accumulation ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Cycle Dependent ◽  
Kinetics Of

scholarly journals Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity.

1997 ◽  
Vol 17 (12) ◽  
pp. 6924-6931 ◽  
Author(s):  
K Sugasawa ◽  
J M Ng ◽  
C Masutani ◽  
T Maekawa ◽  
A Uchida ◽  
...  
Keyword(s):  
Excision Repair ◽  
Early Stage ◽  
Dna Lesions ◽  
Repair Protein ◽  
Nucleotide Excision ◽  
Repair Activity ◽  
In Vitro Repair ◽  
Stimulation Of ◽  
Active Genes

XPC-hHR23B protein complex is specifically involved in nucleotide excision repair (NER) of DNA lesions on transcriptionally inactive sequences as well as the nontranscribed strand of active genes. Here we demonstrate that not only highly purified recombinant hHR23B (rhHR23B) but also a second human homolog of the Saccharomyces cerevisiae Rad23 repair protein, hHR23A, stimulates the in vitro repair activity of recombinant human XPC (rhXPC), revealing functional redundancy between these human Rad23 homologs. Coprecipitation experiments with His-tagged rhHR23 as well as sedimentation velocity analysis showed that both rhHR23 proteins in vitro reconstitute a physical complex with rhXPC. Both complexes were more active than free rhXPC, indicating that complex assembly is required for the stimulation. rhHR23B was shown to stimulate an early stage of NER at or prior to incision. Furthermore, both rhHR23 proteins function in a defined NER system reconstituted with purified proteins, indicating direct involvement of hHR23 proteins in the DNA repair reaction via interaction with XPC.

Structural Insights into the Recognition of N 2 -Aryl- and C8-Aryl DNA Lesions by the Repair Protein XPA/Rad14

ChemBioChem ◽  
2017 ◽  
Vol 18 (14) ◽  
pp. 1379-1382 ◽  
Author(s):  
Charlotte Ebert ◽  
Nina Simon ◽  
Sabine Schneider ◽  
Thomas Carell
Keyword(s):  
Dna Lesions ◽  
Repair Protein ◽  
Structural Insights

scholarly journals Quantitating repair protein accumulation at DNA lesions: Past, present, and future

DNA Repair ◽  
2019 ◽  
Vol 81 ◽  
pp. 102650 ◽  
Author(s):  
Jyothi Mahadevan ◽  
Samuel Bowerman ◽  
Karolin Luger
Keyword(s):  
Dna Lesions ◽  
Protein Accumulation ◽  
Repair Protein

scholarly journals Human MMS21/NSE2 Is a SUMO Ligase Required for DNA Repair

2005 ◽  
Vol 25 (16) ◽  
pp. 7021-7032 ◽  
Author(s):  
Patrick Ryan Potts ◽  
Hongtao Yu
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Ectopic Expression ◽  
Well Being ◽  
Dna Lesions ◽  
Wild Type ◽  
Sumo Ligase ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Induced Apoptosis

ABSTRACT DNA repair is required for the genomic stability and well-being of an organism. In yeasts, a multisubunit complex consisting of SMC5, SMC6, MMS21/NSE2, and other non-SMC proteins is required for DNA repair through homologous recombination. The yeast MMS21 protein is a SUMO ligase. Here we show that the human homolog of MMS21 is also a SUMO ligase. hMMS21 stimulates sumoylation of hSMC6 and the DNA repair protein TRAX. Depletion of hMMS21 by RNA interference (RNAi) sensitizes HeLa cells toward DNA damage-induced apoptosis. Ectopic expression of wild-type hMMS21, but not its ligase-inactive mutant, rescues this hypersensitivity of hMMS21-RNAi cells. ATM/ATR are hyperactivated in hMMS21-RNAi cells upon DNA damage. Consistently, hMMS21-RNAi cells show an increased number of phospho-CHK2 foci. Finally, we show that hMMS21-RNAi cells show a decreased capacity to repair DNA lesions as measured by the comet assay. Our findings suggest that the human SMC5/6 complex and the SUMO ligase activity of hMMS21 are required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair in human cells.

SAC3B is a target of CML19, the centrin 2 of Arabidopsis thaliana

2020 ◽  
Vol 477 (1) ◽  
pp. 173-189 ◽  
Author(s):  
Marco Pedretti ◽  
Carolina Conter ◽  
Paola Dominici ◽  
Alessandra Astegno
Keyword(s):  
Excision Repair ◽  
Complex Structure ◽  
Binding Motif ◽  
C Terminus ◽  
Repair Protein ◽  
Nucleotide Excision ◽  
Ef Hand ◽  
Molecular Determinants ◽  
Structure In Solution

Arabidopsis centrin 2, also known as calmodulin-like protein 19 (CML19), is a member of the EF-hand superfamily of calcium (Ca2+)-binding proteins. In addition to the notion that CML19 interacts with the nucleotide excision repair protein RAD4, CML19 was suggested to be a component of the transcription export complex 2 (TREX-2) by interacting with SAC3B. However, the molecular determinants of this interaction have remained largely unknown. Herein, we identified a CML19-binding site within the C-terminus of SAC3B and characterized the binding properties of the corresponding 26-residue peptide (SAC3Bp), which exhibits the hydrophobic triad centrin-binding motif in a reversed orientation (I8W4W1). Using a combination of spectroscopic and calorimetric experiments, we shed light on the SAC3Bp–CML19 complex structure in solution. We demonstrated that the peptide interacts not only with Ca2+-saturated CML19, but also with apo-CML19 to form a protein–peptide complex with a 1 : 1 stoichiometry. Both interactions involve hydrophobic and electrostatic contributions and include the burial of Trp residues of SAC3Bp. However, the peptide likely assumes different conformations upon binding to apo-CML19 or Ca2+-CML19. Importantly, the peptide dramatically increases the affinity for Ca2+ of CML19, especially of the C-lobe, suggesting that in vivo the protein would be Ca2+-saturated and bound to SAC3B even at resting Ca2+-levels. Our results, providing direct evidence that Arabidopsis SAC3B is a CML19 target and proposing that CML19 can bind to SAC3B through its C-lobe independent of a Ca2+ stimulus, support a functional role for these proteins in TREX-2 complex and mRNA export.

Long-term efficacy of a new medical device containing Fernblock® and DNA repair enzyme complex in the treatment and prevention of cancerization field in patients with actinic keratosis.

2019 ◽  
Vol 2 (02) ◽  
pp. 80-89
Author(s):  
Blanca De Unamuno Bustos ◽  
Natalia Chaparr´´o Aguilera ◽  
Inmaculada Azorín García ◽  
Anaid Calle Andrino ◽  
Margarita Llavador Ros ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Medical Device ◽  
Actinic Keratosis ◽  
Statistical Significance ◽  
Dna Lesions ◽  
Enzyme Complex ◽  
Repair Enzyme ◽  
P53 Expression ◽  
Cancerization Field

Actinic keratosis (AKs) are part of the cancerization field, a region adjacent to AKs containing subclinical and histologically abnormal epidermal tissue due to Ultraviolet (UV)-induced DNA damage. The photoproducts as consequence of DNA damage induced by UV are mainly cyclobutane pyrimidine dimers (CPDs). Fernblock® demonstrated in previous studies significant reduction of the number of CPDs induced by UV radiation. Photolyases are a specific group of enzymes that remove the major UV-induced DNA lesions by a mechanism called photo-reactivation. A monocentric, prospective, controlled, and double blind interventional study was performed to evaluate the effect of a new medical device (NMD) containing a DNA-repair enzyme complex (photolyases, endonucleases and glycosilases), a combination of UV-filters, and Fernblock® in the treatment of the cancerization field in 30 AK patients after photodynamic therapy. Patients were randomized into two groups: patients receiving a standard sunscreen (SS) andpatients receiving the NMD. Clinical, dermoscopic, reflectance confocal microscopy (RCM) and histological evaluations were performed. An increase of AKs was noted in all groups after three months of PDT without significant differences between them (p=0.476). A significant increase in the number of AKs was observed in SS group after six (p=0.026) and twelve months of PDT (p=0.038); however, this increase did not reach statistical significance in the NMD group. Regarding RCM evaluation, honeycomb pattern assessment after twelve months of PDT showed significant differences in the extension and grade of the atypia in the NMD group compared to SS group (p=0.030 and p=0.026, respectively). Concerning histopathological evaluation, keratinocyte atypia grade improved from baseline to six months after PDT in all the groups, with no statistically significant differences between the groups. Twelve months after PDT, p53 expression was significantly lower in the NMD group compared to SS group (p=0.028). The product was well-tolerated, with no serious adverse events reported. Our results provide evidence of the utility of this NMD in the improvement of the cancerization field and in the prevention of the development of new AKs.  

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