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- Title
Interaction of nucleotide excision repair protein XPC-RAD23B with DNA containing benzo[a]pyrene-derived adduct and apurinic/apyrimidinic site within a cluster.
- Authors
Starostenko, L.; Maltseva, E.; Lebedeva, N.; Pestryakov, P.; Lavrik, O.; Rechkunova, N.
- Abstract
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 damage recognition with DNA duplexes containing a B[a]P-derived residue linked to the exocyclic amino group of a guanine (BPDE-N-dG) in the central position of one strand and AP site in different positions of the other strand was analyzed. It was found that XPC-RAD23B crosslinks to DNA containing (+)- trans-BPDE-N-dG more effectively than to DNA containing cis-isomer, independently of the AP site position in the opposite strand; protein affinity to DNA containing one of the BPDE-N-dG isomers depends on the AP site position in the opposite strand. The influence of XPC-RAD23B on hydrolysis of an AP site clustered with BPDE-N-dG catalyzed by the apurinic/apyrimidinic endonuclease 1 (APE1) was examined. XPC-RAD23B was shown to stimulate the endonuclease and inhibit the 3′-5′ exonuclease activity of APE1. These data demonstrate the possibility of cooperation of two proteins belonging to different DNA repair systems in the repair of cluster-type DNA damage.
- Subjects
DNA repair; SURGICAL excision; NUCLEOTIDES; BENZOPYRENE; APURINIC acid; ENDONUCLEASES
- Publication
Biochemistry (00062979), 2016, Vol 81, Issue 3, p233
- ISSN
0006-2979
- Publication type
Article
- DOI
10.1134/S0006297916030056