2013 Fiscal Year Final Research Report
Functions of intrinsically disordered regions in homologous recombination
| Project Area | Target recognition and expression mechanism of intrinsically disordered protein |
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| Project/Area Number |
21113004
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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 | The Institute of Physical and Chemical Research |
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Principal Investigator |
SHIBATA Takehiko 独立行政法人理化学研究所, 遺伝制御科学特別研究ユニット, ユニットリーダー (70087550)
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| Co-Investigator(Kenkyū-buntansha) |
KUSANO Kohji 京都工芸繊維大学, 遺伝資源キュレーター教育研究センター, 特任教授 (70336098)
ARAI Naoto 日本大学, 生物資源科学部, 講師 (70297795)
KAGAWA Wataru 明星大学, 理工学部, 准教授 (70415123)
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| Co-Investigator(Renkei-kenkyūsha) |
INOUE Jin 独立行政法人理化学研究所, 基幹研究所, 特別研究員 (10469893)
KIKAWA Tsutomu 独立行政法人理化学研究所, 遺伝制御科学特別研究ユニット, 専任研究員 (20321820)
LING Feng 独立行政法人理化学研究所, 吉田化学遺伝学研究室, 研究員 (70281665)
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| Project Period (FY) |
2009-07-23 – 2014-03-31
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| Keywords | 天然変性領域 / 相同DNA組換え / 体細胞組換え / LOH / Rad52 組換えメディエーター / RecA族組換え酵素 / Srs2 DNAヘリカーゼ / Rad51 組換え酵素 |
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| Research Abstract |
Degeneration of homologous DNA recombination causes cancer and other diseases. We studied the functions of intrinsically disordered regions (IDRs) of Rad52 and Srs2, and their interactions with a RecA-family recombinase, Rad51, and other related proteins. Using mutagenesis, we identified amino acid-residues in the IDRs of Rad52 and Srs2, which are involved in the interaction with Rad51. A key finding from these studies is that Srs2 functions to facilitate the accurate repair of double-strand breaks without loss of heterozygosity in diploid mitotic cells. Our results further suggest a revision of double-strand-break repair model first proposed Szostak et al (1983). The proposed model includes the repair DNA synthesis-free capture of the processed single-strand DNA tail from the second end of the same double-strand break (Miura et al. PNAS 2013).
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[Journal Article] Functional analyses of the C terminal half of the Saccharomyces cerevisiae Rad52 protein2014
Author(s)
Kagawa, W., Arai, N., Ichikawa, Y., Saito, K., Sugiyama, S., Saotome, M., Shibata, T. and Kurumizaka, H.
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Journal Title
Nucleic Acids Res.
Volume: 42
Pages: 941-951
Peer Reviewed
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[Journal Article] Homologous pairing activities of two rice RAD51 proteins, RAD51A1 and RAD51A22013
Author(s)
Morozumi, Y., Ino, R., Ikawa, S., Mimida, N., Shimizu, T., Toki, S., Ichikawa, H., Shibata, T. and Kurumizaka, H.
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Journal Title
PLoS ONE
Volume: 8
Pages: e75451 (75410)
DOI
Peer Reviewed
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[Journal Article] Homologous recombination via synthesis-dependent strand annealing in yeast requires the Irc20 and Srs2 DNA helicases2012
Author(s)
Miura, T., Yamana, Y., Usui, T., Ogawa, H. I., Yamamoto, M.-T. and Kusano, K.
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Journal Title
Genetics
Volume: 191
Pages: 65-78
Peer Reviewed
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[Journal Article] Vital roles of the second DNA-binding site of Rad52 protein in yeast homologous recombination2011
Author(s)
Arai, N., Kagawa, W., Saito, K., Shingu, Y., Mikawa, T., Kurumizaka, H. and Shibata, T.
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Journal Title
J. Biol. Chem.
Volume: 286
Pages: 17607-17617
DOI
Peer Reviewed
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[Journal Article] A mechanism for single-stranded DNA-binding protein (SSB) displacement from single-stranded DNA upon SSB-RecO interaction2011
Author(s)
Inoue, J., Nagae, T., Mishima, M., Ito, Y., Shibata, T. and Mikawa, T.
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Journal Title
J. Biol. Chem.
Volume: 286
Pages: 6720-6732
Peer Reviewed
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[Journal Article] DIDS, a chemical compound that inhibits RAD51-mediated homologous pairing and strand exchange2009
Author(s)
Ishida, T., Takizawa, Y., Kainuma, T., Inoue, J., Mikawa, T., Shibata, T., Suzuki, H., Tashiro, S. and Kurumizaka, H.
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Journal Title
Nucleic Acids Res.
Volume: 37
Pages: 3367-3376
Peer Reviewed
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