Nadejda I. Rechkunova

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Tyrosyl-DNA phosphodiesterase 1 (Tdp1) catalyzes the hydrolysis of the phosphodiester linkage between the DNA 3' phosphate and a tyrosine residue as well as a variety of other DNA 3' damaged termini. Recently we have shown that Tdp1 can liberate the 3' DNA phosphate termini from apurinic/apyrimidinic (AP) sites. Here, we found that Tdp1 is more active in(More)
The interaction of xeroderma pigmentosum group A protein (XPA) and replication protein A (RPA) with damaged DNA in nucleotide excision repair (NER) was studied using model dsDNA and bubble-DNA structure with 5-{3-[6-(carboxyamido-fluoresceinyl)amidocapromoyl]allyl}-dUMP lesions in one strand and containing photoreactive 5-iodo-dUMP residues in defined(More)
We have examined the influence of centrin 2 (Cen2) on the interaction of nucleotide excision repair factors (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes bearing the dUMP derivative 5-{3-[6-(carboxyamidofluores-ceinyl)amidocapromoyl]allyl}-2′-deoxyuridine-5′-monophosphate. The fluorescein residue linked to the nucleotide base imitates a bulky lesion of(More)
The interaction of nucleotide excision repair (NER) proteins (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes containing the bulky lesion-mimicking fluorescein-substituted derivative of dUMP (5-{3-[6-(carboxyamidofluo-resceinyl)amidocapromoyl]allyl}-2′-deoxyuridine-5′-monophosphate) in a cluster with a lesion of another type (apurinic/apyrimidinic (AP)(More)
26 The genetic stability of a living organism is largely determined by the functioning of DNA repair systems. The regulation of activity of repair processes is an important factor in maintaining the required level of genome protection under genotoxic exposure. One of the key mechanisms of DNA repair regulation is polyy (ADPPribosyl)ation of proteins—a(More)
Replication protein A (RPA) is a key regulator of eukaryotic DNA metabolism. RPA is a highly conserved heterotrimeric protein and contains multiple oligonucleotide/oligosaccharide-binding folds. The major RPA function is binding to single-stranded DNA (ssDNA) intermediates forming in DNA replication, repair, and recombination. Although binding ssDNA with(More)
The combined action of reactive metabolites of benzo[a]pyrene (B[a]P) and oxidative stress can lead to cluster-type DNA damage that includes both a bulky lesion and an apurinic/apyrimidinic (AP) site, which are repaired by the nucleotide and base excision repair mechanisms — NER and BER, respectively. Interaction of NER protein XPC—RAD23B providing primary(More)
Genomic DNA is constantly damaged by the action of exogenous factors and endogenous reactive metabolites. The most common damage in DNA is to apurinic/apyrimidinic sites (AP sites), which are induced by DNA glycosylases or occur as a result of spontaneous hydrolysis of the N-glycosidic bonds. The chemical reactivity of AP sites is the cause of DNA breaks(More)
Xeroderma pigmentosum factor A (XPA) is one of the key proteins in the nucleotide excision repair (NER) process. The effects of point substitutions in the DNA-binding domain of XPA (positively charged lysine residues replaced by negatively charged glutamate residues: XPA K204E, K179E, K141E, and tandem mutant K141E/K179E) on the inter-action of the protein(More)
68 TyrosyllDNA phosphodiesterase 1 (Tdp1) is an enzyme that prevents the accumulation of covalent adducts of topoisomerase I (Top1) with DNA, it hydrolyzes 3''phosphotirosyl bonds [1]. Human Tdp1 can also remove other modifying groups from the 3'' end of DNA (e.g., 3''phosphoglycolates and deoxyrii bose residues); i.e., it functions as a 3''phosphodii(More)