Human DNA polymerase ε is phosphorylated at serine-1940 after DNA damage and interacts with the iron-sulfur complex chaperones CIAO1 and MMS19.
We describe a dynamic phosphorylation on serine-1940 of the catalytic subunit of human Pol ε, POLE1, following DNA damage. We also describe novel interactions between POLE1 and the iron-sulfur cluster assembly complex CIA proteins CIAO1 and MMS19. We show that serine-1940 is essential for the interaction between POLE1 and MMS19, ... but not POLE1 and CIAO1. No defect in either proliferation or survival was identified when POLE1 serine-1940 was mutated to alanine in human cells, even following treatment with DNA damaging agents. We conclude that serine-1940 phosphorylation and the interaction between serine-1940 and MMS19 are not essential functions in the C terminal domain of the catalytic subunit of DNA polymerase ε.
Mesh Terms:
Alanine, Amino Acid Substitution, Cell Line, Tumor, Cell Proliferation, Cell Survival, DNA, DNA Damage, DNA Polymerase II, DNA Repair, HEK293 Cells, Humans, Iron-Sulfur Proteins, Metallochaperones, Mutation, Osteoblasts, Phosphorylation, Poly-ADP-Ribose Binding Proteins, Protein Subunits, Serine, Transcription Factors
Alanine, Amino Acid Substitution, Cell Line, Tumor, Cell Proliferation, Cell Survival, DNA, DNA Damage, DNA Polymerase II, DNA Repair, HEK293 Cells, Humans, Iron-Sulfur Proteins, Metallochaperones, Mutation, Osteoblasts, Phosphorylation, Poly-ADP-Ribose Binding Proteins, Protein Subunits, Serine, Transcription Factors
DNA Repair (Amst.)
Date: Dec. 01, 2015
PubMed ID: 27235625
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