Structural basis for the molecular interactions in DNA damage tolerances

Author:

Hashimoto Hiroshi1,Hishiki Asami1,Hara Kodai1,Kikuchi Sotaro12

Affiliation:

1. School of Pharmaceutical Sciences, University of Shizuoka

2. Department of Pharmacology, University of Texas Southwestern Medical Center

Publisher

Biophysical Society of Japan

Subject

General Medicine

Reference14 articles.

1. [1] Branzei, D. & Psakhye, I. DNA damage tolerance. Curr. Opin. Cell. Biol. 40, 137–144 (2016).

2. [6] Hishiki, A., Hashimoto, H., Hanafusa, T., Kamei, K., Ohashi, E., Shimizu, T., et al. Structural basis for novel interactions between human translesion synthesis polymerases and proliferating cell nuclear antigen. J. Biol. Chem. 284, 10552–10560 (2009).

3. [7] Hara, K., Hashimoto, H., Murakumo, Y., Kobayashi, S., Kogame, T., Unzai, S., et al. Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1. J. Biol. Chem. 285, 12299–12307 (2010).

4. [11] Kikuchi, S., Hara, K., Shimizu, T., Sato, M. & Hashimoto, H. Structural basis of recruitment of DNA polymerase ζ by interaction between REV1 and REV7 proteins. J. Biol. Chem. 287, 33847–33852 (2012).

5. [12] Xie, W., Yang, X., Xu, M. & Jiang, T. Structural insights into the assembly of human translesion polymerase complexes. Protein Cell 3, 864–874 (2012).

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