scholarly journals Inefficient Nucleotide Excision Repair in Human Cell Extracts of theN-(Deoxyguanosin-8-yl)-6-aminochrysene and 5-(Deoxyguanosin-N2-yl)-6-aminochrysene Adducts Derived from 6-Nitrochrysene

2011 ◽  
Vol 24 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Jacek Krzeminski ◽  
Konstantin Kropachev ◽  
Marina Kolbanovskiy ◽  
Dara Reeves ◽  
Alexander Kolbanovskiy ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Human Cell ◽  
Excision Repair ◽  
Cell Extracts ◽  
Nucleotide Excision

scholarly journals Comparative analyses of two primate species diverged by more than 60 million years show different rates but similar distribution of genome-wide UV repair events

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Umit Akkose ◽  
Veysel Ogulcan Kaya ◽  
Laura Lindsey-Boltz ◽  
Zeynep Karagoz ◽  
Adam D. Brown ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Cell Lines ◽  
Human Cell ◽  
Excision Repair ◽  
Mouse Lemur ◽  
Repair Mechanism ◽  
Damage Repair ◽  
Genome Wide ◽  
Repair Efficiency ◽  
Nucleotide Excision

Abstract Background Nucleotide excision repair is the primary DNA repair mechanism that removes bulky DNA adducts such as UV-induced pyrimidine dimers. Correspondingly, genome-wide mapping of nucleotide excision repair with eXcision Repair sequencing (XR-seq), provides comprehensive profiling of DNA damage repair. A number of XR-seq experiments at a variety of conditions for different damage types revealed heterogenous repair in the human genome. Although human repair profiles were extensively studied, how repair maps vary between primates is yet to be investigated. Here, we characterized the genome-wide UV-induced damage repair in gray mouse lemur, Microcebus murinus, in comparison to human. Results We derived fibroblast cell lines from mouse lemur, exposed them to UV irradiation, and analyzed the repair events genome-wide using the XR-seq protocol. Mouse lemur repair profiles were analyzed in comparison to the equivalent human fibroblast datasets. We found that overall UV sensitivity, repair efficiency, and transcription-coupled repair levels differ between the two primates. Despite this, comparative analysis of human and mouse lemur fibroblasts revealed that genome-wide repair profiles of the homologous regions are highly correlated, and this correlation is stronger for highly expressed genes. With the inclusion of an additional XR-seq sample derived from another human cell line in the analysis, we found that fibroblasts of the two primates repair UV-induced DNA lesions in a more similar pattern than two distinct human cell lines do. Conclusion Our results suggest that mouse lemurs and humans, and possibly primates in general, share a homologous repair mechanism as well as genomic variance distribution, albeit with their variable repair efficiency. This result also emphasizes the deep homologies of individual tissue types across the eukaryotic phylogeny.

scholarly journals 8-Oxo-7,8-Dihydroguanine Is Removed by a Nucleotide Excision Repair-Like Mechanism in Porphyromonas gingivalis W83

2004 ◽  
Vol 186 (22) ◽  
pp. 7697-7703 ◽  
Author(s):  
N. A. Johnson ◽  
R. McKenzie ◽  
L. McLean ◽  
L. C. Sowers ◽  
H. M. Fletcher
Keyword(s):  
Oxidative Stress ◽  
Nucleotide Excision Repair ◽  
Porphyromonas Gingivalis ◽  
Excision Repair ◽  
Periodontal Pocket ◽  
Periodontal Pathogens ◽  
Chromosomal Dna ◽  
Inflammatory Microenvironment ◽  
Cell Extracts ◽  
Nucleotide Excision

ABSTRACT A consequence of oxidative stress is DNA damage. The survival of Porphyromonas gingivalis in the inflammatory microenvironment of the periodontal pocket requires an ability to overcome oxidative stress caused by reactive oxygen species (ROS). 8-Oxo-7,8-dihydroguanine (8-oxoG) is typical of oxidative damage induced by ROS. There is no information on the presence of 8-oxoG in P. gingivalis under oxidative stress conditions or on a putative mechanism for its repair. High-pressure liquid chromatography with electrochemical detection analysis of chromosomal DNA revealed higher levels of 8-oxoG in P. gingivalis FLL92, a nonpigmented isogenic mutant, than in the wild-type strain. 8-OxoG repair activity was also increased in cell extracts from P. gingivalis FLL92 compared to those from the parent strain. Enzymatic removal of 8-oxoG was catalyzed by a nucleotide excision repair (NER)-like mechanism rather than the base excision repair (BER) observed in Escherichia coli. In addition, in comparison with other anaerobic periodontal pathogens, the removal of 8-oxoG was unique to P. gingivalis. Taken together, the increased 8-oxoG levels in P. gingivalis FLL92 could further support a role for the hemin layer as a unique mechanism in oxidative stress resistance in this organism. In addition, this is the first observation of an NER-like mechanism as the major mechanism for removal of 8-oxoG in P. gingivalis.

scholarly journals UV radiation-induced SUMOylation of DDB2 regulates nucleotide excision repair

2017 ◽  
Vol 38 (10) ◽  
pp. 976-985 ◽  
Author(s):  
Chunhua Han ◽  
Ran Zhao ◽  
John Kroger ◽  
Jinshan He ◽  
Gulzar Wani ◽  
...  
Keyword(s):  
Dna Damage ◽  
Nucleotide Excision Repair ◽  
Uv Radiation ◽  
Uv Irradiation ◽  
Excision Repair ◽  
26S Proteasome ◽  
Cell Extracts ◽  
Nucleotide Excision

Abstract Subunit 2 of DNA damage-binding protein complex (DDB2) is an early sensor of nucleotide excision repair (NER) pathway for eliminating DNA damage induced by UV radiation (UVR) and cisplatin treatments of mammalian cells. DDB2 is modified by ubiquitin and poly(ADP-ribose) (PAR) in response to UVR, and these modifications play a crucial role in regulating NER. Here, using immuno-analysis of irradiated cell extracts, we have identified multiple post-irradiation modifications of DDB2 protein. Interestingly, although the DNA lesions induced by both UVR and cisplatin are corrected by NER, only the UV irradiation, but not the cisplatin treatment, induces any discernable DDB2 modifications. We, for the first time, show that the appearance of UVR-induced DDB2 modifications depend on the binding of DDB2 to the damaged chromatin and the participation of functionally active 26S proteasome. The in vitro and in vivo analysis revealed that SUMO-1 conjugations comprise a significant portion of these UVR-induced DDB2 modifications. Mapping of SUMO-modified sites demonstrated that UVR-induced SUMOylation occurs on Lys-309 residue of DDB2 protein. Mutation of Lys-309 to Arg-309 diminished the DDB2 SUMOylation observable both in vitro and in vivo. Moreover, K309R mutated DDB2 lost its function of recruiting XPC to the DNA damage sites, as well as the ability to repair cyclobutane pyrimidine dimers following cellular UV irradiation. Taken together, our results indicate that DDB2 is modified by SUMOylation upon UV irradiation, and this post-translational modification plays an important role in the initial recognition and processing of UVR-induced DNA damage occurring within the context of chromatin.

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