Biochemistry (Moscow)

, Volume 73, Issue 9, pp 1042–1046 | Cite as

Interaction between DNA polymerase λ and RPA during translesion synthesis

  • Yu. S. Krasikova
  • E. A. Belousova
  • N. A. Lebedeva
  • P. E. Pestryakov
  • O. I. LavrikEmail author


Replication of damaged DNA (translesion synthesis, TLS) is realized by specialized DNA polymerases. Additional protein factors such as replication protein A (RPA) play important roles in this process. However, details of the interaction are unknown. Here we analyzed the influence of the hRPA and its mutant hABCD lacking domains responsible for protein-protein interactions on ability of DNA polymerase λ to catalyze TLS. The primer-template structures containing varying parts of extended strand (16 and 37 nt) were used as model systems imitating DNA intermediate of first stage of TLS. The 8-oxoguanine disposed in +1 position of the template strand in relation to 3′-end of primer was exploited as damage. It was shown that RPA stimulated TLS DNA synthesis catalyzed by DNA polymerase λ in its globular but not in extended conformation. Moreover, this effect is dependent on the presence of p70N and p32C domains in RPA molecule.

Key words

DNA replication translesion DNA synthesis DNA polymerase λ replication protein A 


AP sites

apurinic/apyrimidinic sites


base excision repair




proliferating cell nuclear antigen


replication protein A


translesion DNA synthesis


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Copyright information

© MAIK Nauka 2008

Authors and Affiliations

  • Yu. S. Krasikova
    • 1
    • 2
  • E. A. Belousova
    • 1
  • N. A. Lebedeva
    • 1
    • 2
  • P. E. Pestryakov
    • 1
  • O. I. Lavrik
    • 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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