Biochemistry (Moscow)

, Volume 81, Issue 3, pp 233–241 | Cite as

Interaction of nucleotide excision repair protein XPC—RAD23B with DNA containing benzo[a]pyrene-derived adduct and apurinic/apyrimidinic site within a cluster

  • L. V. Starostenko
  • E. A. Maltseva
  • N. A. Lebedeva
  • P. E. Pestryakov
  • O. I. Lavrik
  • N. I. RechkunovaEmail author


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-N2-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-N2-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-N2-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-N2-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.

Key words

protein factors of nucleotide excision repair benzo[a]pyrene derivatives apurinic/apyrimidinic site cluster-type DNA damage affinity labeling DNA–protein complexes 



apurinic/apyrimidinic endonuclease 1

AP site

apurinic/apyrimidinic site




base excision repair


benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide-N2-deoxyguanosine adduct (in DNA)


nucleotide excision repair


polycyclic aromatic hydrocarbons




xeroderma pigmentosum factor of complementation group A


xeroderma pigmentosum factor of complementation group C in complex with homolog of yeast Rad23 protein


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Copyright information

© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  • L. V. Starostenko
    • 1
  • E. A. Maltseva
    • 1
  • N. A. Lebedeva
    • 1
    • 2
  • P. E. Pestryakov
    • 1
  • O. I. Lavrik
    • 1
    • 2
  • N. I. Rechkunova
    • 1
    • 2
    Email author
  1. 1.Institute of Chemical Biology and Fundamental MedicineSiberian Branch of the Russian Academy of SciencesNovosibirskRussia
  2. 2.Novosibirsk State UniversityNovosibirskRussia

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