EMBO Rep. 2013 Oct 15. [Epub ahead of print]
Li Wan, Jiangman Lou, Yisui Xia, Bei Su, Ting Liu, Jiamin Cui, Yingying Sun, Huiqiang Lou, Jun Huang*
Abstract
Prim-pol is a recently identified DNAprimase-polymerase belonging to the archaeao-eukaryotic primase (AEP) superfamily. Here, we characterize a previously unrecognized prim-pol in human cells, which we designate hPrimpol1 (humanprimase-polymerase 1). hPrimpol1 possesses primase and DNA polymerase activities in vitro, interacts directly with RPA1 and is recruited to sites of DNA damage and stalled replication forks in an RPA1-dependent manner. Cells depleted of hPrimpol1 display increased spontaneous DNA damage and defects in the restart of stalled replication forks. Both RPA1 binding and the primase activity of hPrimpol1 are required for its cellular function during DNA replication. Our results indicate that hPrimpol1 is a novel factor involved in the response to DNA replication stress.
Text link：http://www.nature.com/embor/journal/vaop/ncurrent/full/embor2013159a.html
