2013 Fiscal Year Final Research Report
Structural study of telomere maintenance mechanism of RecQ helicases
Project/Area Number |
23770118
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | Nara Institute of Science and Technology |
Principal Investigator |
KITANO Ken 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (40346309)
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Project Period (FY) |
2011 – 2012
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Keywords | タンパク質 / DNA ヘリカーゼ / RecQ ファミリー / X線結晶解析 / 構造生物学 / 生物物理学 / 三量体Gタンパク質 / 阻害剤 |
Research Abstract |
RecQ family of DNA helicases WRN (Werner syndrome protein) and BLM (Bloom syndrome protein) play a key role in protecting the genome against deleterious changes. In this study, we determined the first three-dimensional structure of a RecQ C-terminal (RQC) domain from human BLM bound to a phosphate ion. Our result gave insights into the unique DNA-unwinding activity of RecQ helicases toward recombination and repair intermediates (Kim, SY., Hakoshima, T., and Kitano, K., 2013, Sci. Rep., 3, 3294.).
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Research Products
(15 results)
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[Presentation] Protein interaction between NADH oxidase and AhpC (Prx) from Amphibacillus xylanus2013
Author(s)
Mochizuki, D., Arai, T., Hara, K., Matsumoto, T., Kitano, K., Zako, T., Okada, M., Yohda, M., Sato, J., Kawasaki, S., Kanamaru, S., Arisaka, F., Niimura, Y.
Organizer
21st International Conference on Analytical Ultracentrifugation, Hydrodynamics, Thermodynamics and Complementary Methods (AUC2013)
Place of Presentation
静岡県熱海市,ホテルニューアカオ
Year and Date
2013-09-26
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[Remarks] Protein Data Bank (PDB)への登録 ①Kim, SY., Hakoshima, T., Kitano, K. (2013), "Structure of BLM RQC domain bound to a phosphate ion." 3WE2.