Systematic analysis on RNA recognition mechanism of PPR protein for plant organelle gene expression
| Project/Area Number |
22681028
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| Research Category |
Grant-in-Aid for Young Scientists (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Genome biology
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| Research Institution | Kyushu University |
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Principal Investigator |
NAKAMURA Takahiro 九州大学, (連合)農学研究科(研究院), 准教授 (10464398)
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| Project Period (FY) |
2010-04-01 – 2013-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥25,220,000 (Direct Cost: ¥19,400,000、Indirect Cost: ¥5,820,000)
Fiscal Year 2012: ¥9,100,000 (Direct Cost: ¥7,000,000、Indirect Cost: ¥2,100,000)
Fiscal Year 2011: ¥8,320,000 (Direct Cost: ¥6,400,000、Indirect Cost: ¥1,920,000)
Fiscal Year 2010: ¥7,800,000 (Direct Cost: ¥6,000,000、Indirect Cost: ¥1,800,000)
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| Keywords | オルガネラゲノム / PPR / RNA / 葉緑体 / ミトコンドリア / PRP蛋白質 / PPR蛋白質 |
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| Research Abstract |
Pentatricopeptide repeat (PPR) proteins are eukaryotic RNA-binding proteins that are commonly found in plants. Organelle transcript processing and stability are mediated by PPR proteins in a gene-specific manner through recognition by tandem arrays of degenerate 35-amino-acid repeating units, the PPR motifs. Here, we showed the principle underlying RNA recognition for PPR proteins involved in RNA editing. Amino acid variation at 3 particular positions within the motif determined recognition of a specific RNA in a programmable manner, with a 1-motif to 1-nucleotide correspondence,. Data from the decoded nucleotide frequencies for these 3 amino acids were used to assign accurate interacting sites to several PPR proteins for RNA editing and to predict the target sites for an uncharacterized PPR proteins. In another view, PPR proteins appear to provide an extremely promising opportunity to create custom RNA binding proteins with tailored specificity.
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Report
(4 results)
Research Products
(47 results)
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[Journal Article] Identification and characterization of the RNA binding surface of the pentatricopeptide repeat protein2012
Author(s)
Kobayashi, K., Kawabata, M., Hisano, K., Kazama, T., Matsuoka, K., Sugita, M., Nakamura, T.
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Journal Title
Nucleic Acids Res.
Volume: 40
Pages: 2712-2723
Related Report
Peer Reviewed
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[Journal Article] Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing2012
Author(s)
Murayama, M., Hayashi, S., Nishimura, N., Ishide, M., Kobayashi, K., Yagi, Y., Asami, T., Nakamura, T., Shinozaki, K., Hirayama, T.
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Journal Title
J. Exp. Bot.
Volume: 63
Pages: 5301-5310
Related Report
Peer Reviewed
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[Journal Article] Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing.2012
Author(s)
Murayama M, Hayashi S, Nishimura N, Ishide M, Kobayashi K, Yagi Y, Asami T, Nakamura T, Shinozaki K, Hirayama T
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Journal Title
J. Exp. Bot.
Volume: 63
Issue: 14
Pages: 5301-5310
DOI
Related Report
Peer Reviewed
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[Journal Article] A plastid protein NUS1 is essential for build-up of the genetic system for early chloroplast development under cold stress conditions2011
Author(s)
Kusumi, K., Sakata, C., Nakamura, T., Kawasaki, S., Yoshimura, A., Iba, K.
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Journal Title
Plant J.
Volume: 68
Pages: 1039-1050
Related Report
Peer Reviewed
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[Journal Article] A plastid protein NUS1 is essential for build-up of the genetic system for early chloroplast development under cold stress conditions2011
Author(s)
Kusumi, K., Sakata, C., Nakamura, T., Kawasaki, S., Yoshimura, A., and Iba, K.
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Journal Title
Plant J.
Volume: 68
Issue: 6
Pages: 1039-1050
DOI
Related Report
Peer Reviewed
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