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Interaction between DNA Polymerase lambda and RPA during Translesion Synthesis

Yu. S. Krasikova1,2, E. A. Belousova1, N. A. Lebedeva1,2, P. E. Pestryakov1, and O. I. Lavrik1,2*

1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Akademika Lavrentieva 8, 630090 Novosibirsk, Russia; fax: (383) 333-3677; E-mail: lavrik@niboch.nsc.ru

2Novosibirsk State University, ul. Pirogova 2, 630090 Novosibirsk, Russia

* To whom correspondence should be addressed.

Received November 13, 2007; Revision received December 28, 2007
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 lambda 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 lambda 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 lambda, replication protein A

DOI: 10.1134/S0006297908090125