人类DNA聚合酶ε在DNA损伤后会在丝氨酸1940处发生磷酸化，并与铁硫复合物伴侣蛋白CIAO1和MMS19相互作用。
Human DNA polymerase ε is phosphorylated at serine-1940 after DNA damage and interacts with the iron-sulfur complex chaperones CIAO1 and MMS19.
作者信息
Moiseeva Tatiana N, Gamper Armin M, Hood Brian L, Conrads Thomas P, Bakkenist Christopher J
机构信息
Department of Radiation Oncology, University of Pittsburgh School of Medicine, Hillman Cancer Center, Research Pavilion, Suite 2.6, 5117 Centre Avenue, Pittsburgh, PA 15213-1863, USA.
Department of Radiation Oncology, University of Pittsburgh School of Medicine, Hillman Cancer Center, Research Pavilion, Suite 2.6, 5117 Centre Avenue, Pittsburgh, PA 15213-1863, USA; Department of Oncology, University of Alberta, Cross Cancer Institute, 11560 University Avenue, Edmonton, AB T6 G 1Z2, Canada.
出版信息
DNA Repair (Amst). 2016 Jul;43:9-17. doi: 10.1016/j.dnarep.2016.04.007. Epub 2016 May 7.
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.
我们描述了DNA损伤后人源Pol ε催化亚基POLE1的丝氨酸1940位点上的动态磷酸化。我们还描述了POLE1与铁硫簇组装复合体CIA蛋白CIAO1和MMS19之间的新型相互作用。我们发现丝氨酸1940对于POLE1与MMS19之间的相互作用至关重要，但对POLE1与CIAO1之间的相互作用并非如此。当人源细胞中POLE1的丝氨酸1940突变为丙氨酸时，即使在用DNA损伤剂处理后，也未发现增殖或存活方面的缺陷。我们得出结论，丝氨酸1940磷酸化以及丝氨酸1940与MMS19之间的相互作用并非DNA聚合酶ε催化亚基C末端结构域的必需功能。
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