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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• 作者：Tatiana N. Moiseeva^a ; Armin M. Gamper^a ; ^b ; Brian L. Hood^c ; Thomas P. Conrads^c ; Christopher J. Bakkenist^a ; ^d ; ^{bakkenistcj@upmc.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：DNA polymerase epsilon ; CIAO1 ; MMS19 ; DNA damage
• 刊名：DNA Repair
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：43
• 期：Complete
• 页码：9-17
• 全文大小：1953 K

文摘

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.