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Human DNA polymerase ε is phosphorylated at serine-1940 after DNA damage and interacts with the iron-sulfur complex chaperones CIAO1 and MMS19.
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- Additional Information
- Source:
Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101139138 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1568-7856 (Electronic) Linking ISSN: 15687856 NLM ISO Abbreviation: DNA Repair (Amst) Subsets: MEDLINE
- Publication Information:
Original Publication: Amsterdam ; New York : Elsevier, c2002-
- Subject Terms:
- Abstract:
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.
(Copyright © 2016 Elsevier B.V. All rights reserved.)
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- Grant Information:
P30 CA047904 United States CA NCI NIH HHS; P50 CA090440 United States CA NCI NIH HHS; R01 CA148644 United States CA NCI NIH HHS; UM1 CA186690 United States CA NCI NIH HHS
- Contributed Indexing:
Keywords: CIAO1; DNA damage; DNA polymerase epsilon; MMS19
- Accession Number:
0 (CIAO1 protein, human)
0 (Iron-Sulfur Proteins)
0 (MMS19 protein, human)
0 (Metallochaperones)
0 (Poly-ADP-Ribose Binding Proteins)
0 (Protein Subunits)
0 (Transcription Factors)
452VLY9402 (Serine)
9007-49-2 (DNA)
EC 2.7.7.7 (DNA Polymerase II)
EC 2.7.7.7 (POLE protein, human)
OF5P57N2ZX (Alanine)
- Publication Date:
Date Created: 20160529 Date Completed: 20170515 Latest Revision: 20201209
- Publication Date:
20240829
- Accession Number:
PMC4917431
- Accession Number:
10.1016/j.dnarep.2016.04.007
- Accession Number:
27235625
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