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Abstract
DNA polymerase iota (Polι) belongs to the Y-family of DNA polymerases that are involved in DNA damage tolerance through their role in translesion DNA synthesis. Like all other Y-family polymerases, Polι interacts with proliferating cell nuclear antigen (PCNA), Rev1, ubiquitin and ubiquitinated-PCNA and is also ubiquitinated itself. Here, we report that Polι also interacts with the p300 acetyltransferase and is acetylated. The primary acetylation site is K550, located in the Rev1-interacting region. However, K550 amino acid substitutions have no effect on Polι’s ability to interact with Rev1. Interestingly, we find that acetylation of Polι significantly and specifically increases in response to SN2 alkylating agents and to a lower extent to SN1 alkylating and oxidative agents. As we have not observed acetylation of Polι’s closest paralogue, DNA polymerase eta (Polη), with which Polι shares many functional similarities, we believe that this modification might exclusively regulate yet to be determined, and separate function(s) of Polι.
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Details
1 Polish Academy of Sciences, ul. Pawinskiego 5a, Institute of Biochemistry and Biophysics, Warsaw, Poland (GRID:grid.413454.3) (ISNI:0000 0001 1958 0162)
2 National Institutes of Health, Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, Bethesda, USA (GRID:grid.94365.3d) (ISNI:0000 0001 2297 5165)
3 International Institute of Molecular and Cell Biology, ul. Ks. Trojdena 4, Laboratory of Molecular and Cellular Neurobiology, Warsaw, Poland (GRID:grid.419362.b)