2013 Fiscal Year Final Research Report
Development of a novel method for structure analysis of intrinsically disordered protein
| Project Area | Target recognition and expression mechanism of intrinsically disordered protein |
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| Project/Area Number |
21113002
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| Research Category |
Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Yokohama City University |
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Principal Investigator |
SATO Mamoru 横浜市立大学, その他の研究科, 教授 (60170784)
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| Co-Investigator(Kenkyū-buntansha) |
ANDO Toshio 金沢大学, 数物科学系, 教授 (50184320)
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| Project Period (FY) |
2009-07-23 – 2014-03-31
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| Keywords | Ｘ線小角散乱 / 高速ＡＦＭ / 分子動力学シミュレーション / マルチドメインタンパク質 / 核内タンパク質 |
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| Research Abstract |
In this study, we have developed novel methods to investigate flexible structure of intrinsically disordered proteins (IDPs) by small-angle X-ray scattering (SAXS) and molecular dynamics (MD) simulation (MD-SAXS) and by high-speed atomic force microscopy (AFM). In the MD-SAXS method, SAXS profile was calculated from the dynamic IDP model calculated considering complementary experimental data, and compared with experimental profile so that they are in agreement with the experimental data. In the high-speed AFM, a new method to reduce the noise level of the AFM device and a solution condition and supporting plate suitable for IDP observation have been developed. Reliability of the AFM has been assessed through the observation of PQBP-1 where NMR analysis went ahead for the identification of IDR. Based on these experiments, we have collaborated with a number of research group within this IDP research project in Japan and elucidated the structure-function relationship of various IDPs.
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Research Products
(36 results)
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[Journal Article] Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin2013
Author(s)
Y.Arimura, H.Kimura, T.Oda, K.Sato, A.Osakabe, H.Tachiwana, Y.Sato, Y.Kinugasa, T.Ikura, M.Sugiyama, M.Sato, and H.Kurumizaka
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Journal Title
Sci. Rep
Volume: 3
Pages: 3510
DOI
Peer Reviewed
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[Journal Article] Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex2013
Author(s)
N.Kuwabara, Y.Murayama, H.Hashimoto, Y.Kokabu, M.Ikeguchi, M.Sato, K.Mayanagi, Y.Tsutsui, H.Iwasaki,and T.Shimizu
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Journal Title
Structure
Volume: 20
Pages: 440-449
DOI
Peer Reviewed
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[Journal Article] Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF12012
Author(s)
K.Arita, S.Isogai, T.Oda, M.Unoki, K.Sugita, N.Sekiyama, K.Kuwata, R.Hamamoto, H.Tochio, M.Sato, M.Ariyoshi, and M.Shirakawa
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Journal Title
Proc. Natl. Acad. Sci. USA
Volume: 109
Pages: 12950-12955
DOI
Peer Reviewed
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[Journal Article] Crystal structure of the human centromeric nucleosome containing CENP-A2011
Author(s)
H.Tachiwana, W.Kagawa, T.Shiga, A.Osakabe, Y.Miya, K.Saito, Y.Hayashi-Takanaka, T.Oda, M.Sato, S.-Y.Park, H.Kimura, and H.Kurumizaka
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Journal Title
Nature
Volume: 476
Pages: 232-235
DOI
Peer Reviewed
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[Journal Article] Fission Yeast Swi5-Sfr1 Protein Complex, an Activator of Rad51 Recombinase, Forms an Extremely Elongated Dogleg-shaped Structure2011
Author(s)
Y.Kokabu, Y.Murayama, N.Kuwabara, T.Oroguchi, H.Hashimoto, Y.Tsutsui, N.Nozaki, S.Akashi, S.Unzai, T.Shimizu, H.Iwasaki, M.Sato, and M.Ikeguchi
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Journal Title
J. Biol. Chem
Volume: 286
Pages: 43569-43576
DOI
Peer Reviewed
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