Interaction between DNA polymerase l and RPA during translesion synthesis

• Published in: Biochemistry (Moscow) Vol. 73; no. 9; pp. 1042 - 1046
• Main Authors: Krasikova, YuS, Belousova, E A, Lebedeva, NA, Pestryakov, P E, Lavrik, OI
• Format: Journal Article
• Language: English
• Published: 01.09.2008
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297908090125

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 l 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 l in its globular but not in extended conformation. Moreover, this effect is dependent on the presence of p70N and p32C domains in RPA molecule.