Interaction between DNA polymerase [lambda] and RPA during translesion synthesis

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...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2008-09, Vol.73 (9), p.1042
Main Authors: Krasikova, Yu S, Belousova, E A, Lebedeva, N A, Pestryakov, P E, Lavrik, O I
Format: Article
Language:English
Subjects:
Biochemistry
Deoxyribonucleic acid
DNA
DNA polymerase
Proteins
Studies
Online Access:Get full text
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Summary: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. (PUBLICATION ABSTRACT)
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297908090125