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E-mail: sycho@cau.ac.krReceived June 11, 2014, Accepted June 18, 2014Human ChlR1 protein (hChlR1), a member of the cohesion establishment factor family, plays an important rolein the segregation of sister chromatids for maintenance of genome integrity. We previously reported thathChlR1 interacts with hFen1 and stimulates its nuclease activity on the flap-structured DNA substrate coveredwith RPA. To elucidate the relationship between hChlR1 and Okazaki fragment processing, the effect ofhChlR1 on in vitro nuclease activities of hFen1 and hDna2 was examined. Independent of ATPase activity,hChlR1 stimulated endonuclease activity of hFen1 but not that of hDna2. Our findings suggest that theacceleration of Okazaki fragment processing near cohesions may aid in reducing the size of the replicationmachinery, thereby facilitating its entry through the cohesin ring.Key Words : ChlR1, Dna2, Fen1, Okazaki fragment processingIntroductionIn eukaryotic cells, DNA replication is initiated at multipleorigins and proceeds bidirectionally from each origin toflanking DNA. For simultaneous synthesis of both strands,the leading strand is continuously replicated by DNA poly-merase e whereas the lagging strand is synthesized as shortOkazaki fragments by primase, DNA polymerases α and δ,and then ligated into one long DNA strand. These enzymesbuild up the replisome in conjunction with other compo-nents, such as Mcm2-7 helicase, PCNA, and RFC.

Human ChlR1 Stimulates Endonuclease Activity of hFen1 Independently of ATPase Activity