Human ChlR1 Stimulates Endonuclease Activity of hFen1 Independently of ATPase Activity 


Vol. 35,  No. 10, pp. 3005-3008, Oct.  2014
10.5012/bkcs.2014.35.10.3005


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  Abstract

Human ChlR1 protein (hChlR1), a member of the cohesion establishment factor family, plays an important role in the segregation of sister chromatids for maintenance of genome integrity. We previously reported that hChlR1 interacts with hFen1 and stimulates its nuclease activity on the flap-structured DNA substrate covered with RPA. To elucidate the relationship between hChlR1 and Okazaki fragment processing, the effect of hChlR1 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 the acceleration of Okazaki fragment processing near cohesions may aid in reducing the size of the replication machinery, thereby facilitating its entry through the cohesin ring.

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  Cite this article

[IEEE Style]

D. Kim, J. Kim, B. C. Park, D. H. Lee, S. Cho, S. G. Park, "Human ChlR1 Stimulates Endonuclease Activity of hFen1 Independently of ATPase Activity," Bulletin of the Korean Chemical Society, vol. 35, no. 10, pp. 3005-3008, 2014. DOI: 10.5012/bkcs.2014.35.10.3005.

[ACM Style]

Do-Hyung Kim, Jeong-Hoon Kim, Byoung Chul Park, Do Hee Lee, Sayeon Cho, and Sung Goo Park. 2014. Human ChlR1 Stimulates Endonuclease Activity of hFen1 Independently of ATPase Activity. Bulletin of the Korean Chemical Society, 35, 10, (2014), 3005-3008. DOI: 10.5012/bkcs.2014.35.10.3005.

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ISSN(Print) 0253-2964
ISSN(Online) 1229-5949