Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages

Maltseva, Ekaterina A.; Rechkunova, N. I.; Gillet, Ludovic; Petruseva, I. O.; Schärer, Orlando D.; Lavrik, Olga I.

doi:10.1016/j.bbagen.2007.01.007

Cited by 29 publications

(23 citation statements)

References 48 publications

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“…The T-T-dimers and the thymine monoadduct of 4 0 -hydroxymethyl-4,5 0 ,8-trimethylpsoralen (T-HMT) are examples of the pyrimidine-lesions used to design artificial DNA structures (Smith and Taylor, 1993;Huang et al, 1994;Mu et al, 1997). Studies are in progress to improve the synthesis and to extend the variety of model DNA lesions (DellaVecchia et al, 2004;Buterin et al, 2005;Gillet et al, 2005;Maltseva et al, 2006;Maltseva et al, 2007). Fluorescein residue and several arylazide groups introduced via (www.interscience.wiley.com) DOI:10.1002/jmr.877…”

Section: Introductionmentioning

confidence: 99%

“…This technique is based on two enzymes action: DNA polymerase beta can use as substrates 4N-dCTP and 5C-dUTP conjugates bearing tethered arylazido groups, whereupon resulting 3 0 -end modified oligonucleotide can be processed with T4 DNA ligase to form DNA fragment, containing photoactive dNMP residue in the internal position (for review see Khodyreva and Lavrik, 2005). Though DNA, containing tethered arylazido lesions have been shown true NER substrates and effective photoactive DNA probes (DellaVecchia et al, 2004;Maltseva et al, 2007), the details of their repair recognition by early NER proteins (XPC, RPA, and XPA) still remain obscure.…”

Section: Introductionmentioning

confidence: 99%

“…different linkers at the nitrogen base moiety of nucleotides have been used in recent investigations to mimic DNA damages produced by action of aromatic hydrocarbons derivatives (DellaVecchia et al, 2004;Tapias et al, 2004;Maltseva et al, 2006;Maltseva et al, 2007). The enzymatic approach to synthesis of artificial DNA structures allows to create NER substrates analogs of any nucleotide sequence and of various architecture easily.…”

Section: Introductionmentioning

confidence: 99%

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RPA repair recognition of DNA containing pyrimidines bearing bulky adducts

Petruseva

Tikhanovich

Челобанов

et al. 2008

J of Molecular Recognition

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Recognition of new DNA nucleotide excision repair (NER) substrate analogs, 48-mer ddsDNA (damaged double-stranded DNA), by human replication protein A (hRPA) has been analyzed using fluorescence spectroscopy and photoaffinity modification. The aim of the present work was to find quantitative characteristics of RPA-ddsDNA interaction and RPA subunits role in this process. The designed DNA structures bear bulky substituted pyrimidine nitrogen bases at the inner positions of duplex forming DNA chains. The photoreactive 4-azido-2,5-difluoro-3- pyridin-6-yl (FAP) and fluorescent antracenyl, pyrenyl (Antr, Pyr) groups were introduced via different linker fragments into exo-4N of deoxycytidine or 5C of deoxyuridine. J-dU-containing DNA was used as a photoactive model of undamaged DNA strands. The reporter group was a fluorescein residue, introduced into the 5'-phosphate end of one duplex-forming DNA strand. RPA-dsDNA association constants and the molar RPA/dsDNA ratio have been calculated based on fluorescence anisotropy measurements under conditions of a 1:1 RPA/dsDNA molar ratio in complexes. The evident preference for RPA binding to ddsDNA over undamaged dsDNA distinctly depends on the adduct type and varies in the following way: undamaged dsDNA < Antr-dC-ddsDNA < mmdsDNA < FAPdU-, Pyr-dU-ddsDNA < FAP-dC-ddsDNA (K(D) = 68 +/- 1; 25 +/- 6; 13 +/- 1; 8 +/- 2, and 3.5 +/- 0.5 nM correspondingly) but weakly depends on the chain integrity. Interestingly the bulkier lesions not in all cases have a greater effect on RPA affinity to ddsDNA. The experiments on photoaffinity modification demonstrated only p70 of compactly arranged RPA directly interacting with dsDNA. The formation of RPA-ddsDNA covalent adducts was drastically reduced when both strands of DNA duplex contained virtually opposite located FAP-dC and Antr-dC. Thus RPA requires undamaged DNA strand presence for the effective interaction with dsDNA bearing bulky damages and demonstrates the early NER factors characteristic features underlying strand discrimination capacity and poor activity of the NER system toward double damaged DNA.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RPA repair recognition of DNA containing pyrimidines bearing bulky adducts

Petruseva

Tikhanovich

Челобанов

et al. 2008

J of Molecular Recognition

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“…6C). We have shown previously that RPA influences XPC-RAD23B modification due to protein-protein interactions (15,20). The level of RPA labeling significantly decreases with the simultaneous appearance of the products of XPC-RAD23B modification.…”

Section: Xpc-rad23b and Rad4-rad23mentioning

confidence: 99%

“…The presence of the acetylaminofluorene adducts or of the loop in the DNA structure caused asymmetrical contacts of XPC-RAD23B with the 5Ј-side of the looped or damaged DNA (12,13). Despite the interaction of XPC with nucleotides surrounding the lesion, photocross-linking experiments were able to detect contacts with the damaged base only in the case of a lesion containing a photoreactive group attached by a long linker (14,15). Further truncation analyses revealed that different XPC structure domains contribute to recognition of different segments of damaged DNA.…”

mentioning

confidence: 99%

Comparative Analysis of Interaction of Human and Yeast DNA Damage Recognition Complexes with Damaged DNA in Nucleotide Excision Repair

Krasikova

Rechkunova

Maltseva

et al. 2013

Journal of Biological Chemistry

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Background: XPC-RAD23B and Rad4-Rad23 proteins are primary damage recognition factors in nucleotide excision repair in human and yeast cells, respectively. Results: XPC-RAD23B and Rad4-Rad23 have contacts with damaged DNA in the same positions. Conclusion: Both proteins reveal similar topography in the complex with damaged DNA in solution.Significance: This study fills the gap between biochemical results for XPC-RAD23B and x-ray data for Rad4-Rad23.

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Novel Diazirine‐Containing DNA Photoaffinity Probes for the Investigation of DNA‐Protein‐Interactions

et al. 2008

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An investigation of the precise interactions between damaged DNA and DNA repair enzymes is required in order to understand the lesion recognition step, which is one of the most fundamental processes in DNA repair. Most recently, photoaffinity labeling approaches have enabled the analysis of even transient protein-DNA interactions. Here we report the synthesis and evaluation of oligonucleotides that contain two photoaffinity "catcher moieties" next to incorporated DNA lesions. With these DNA constructs it is possible to analyze the interactions between DNA lesions and the appropriate repair enzymes. The probes labeled the repair protein efficiently enough to enable subsequent protein analysis by mass spectrometry.

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Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages

Cited by 29 publications

References 48 publications

RPA repair recognition of DNA containing pyrimidines bearing bulky adducts

RPA repair recognition of DNA containing pyrimidines bearing bulky adducts

Comparative Analysis of Interaction of Human and Yeast DNA Damage Recognition Complexes with Damaged DNA in Nucleotide Excision Repair

Novel Diazirine‐Containing DNA Photoaffinity Probes for the Investigation of DNA‐Protein‐Interactions

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