Accepted_test

Human REV1 catalytic activity
by Stolyarenko Anastasia | Novikova Anna | Shilkin Evgeniy | Kruchinin Alexander | Makarova Alena | 1 National Research Center “Kurchatov Institute”, 123182 Moscow, Russia 2 Institute of Gene Biology of the Russian Academy of Sciences, 119334 Moscow, Russia | 1 National Research Center “Kurchatov Institute”, 123182 Moscow, Russia 2 Institute of Gene Biology of the Russian Academy of Sciences, 119334 Moscow, Russia | 1 National Research Center “Kurchatov Institute”, 123182 Moscow, Russia 2 Institute of Gene Biology of the Russian Academy of Sciences, 119334 Moscow, Russia | 1 National Research Center “Kurchatov Institute”, 123182 Moscow, Russia 2 Institute of Gene Biology of the Russian Academy of Sciences, 119334 Moscow, Russia | 1 National Research Center “Kurchatov Institute”, 123182 Moscow, Russia 2 Institute of Gene Biology of the Russian Academy of Sciences, 119334 Moscow, Russia
Abstract ID: 783
Event: BGRS-abstracts
Sections: [Sym 11] Section “DNA replication and repair”

Conserved eukaryotic REV1 serves as a scaffold protein for the coordination of DNA polymerases during DNA translesion synthesis. Besides this structural role, REV1 is a Y-family DNA polymerase with its own distributive deoxycytidyl transferase activity.

The preferable template of REV1 is known to be G. We studied REV1 replication of the most frequent lesion of G, 8-oxoG, with contradictory data in the literature and showed that REV1 is inhibited over 360 fold.

By using the 1,N6-ethenoA lesion and 7-deazaA modification, we provide biochemical evidence of the importance for human REV1 functioning of the Hoogsteen face of template A, the second preferable template after G. Also, we studied 8-oxoA for the first time and showed that it was replicated by REV1 in an error-prone manner.

Among the lesions of pyrimidines, the least favorite templates of REV1, methylC and hydroxymethylC inhibited REV1. Surpisingly, thymine glycol was replicated in an error-prone manner over 1700-fold more efficiently than undamaged T.

The study is supported by the state task of the National Research Center "Kurchatov Institute".