2013 Fiscal Year Final Research Report
Biochemical identification of RNA editing enzyme in plastids
| Project/Area Number |
23657032
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Plant molecular biology/Plant physiology
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2012
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| Keywords | 葉緑体 / RNA / PPRタンパク質 / 翻訳 / 光合成 |
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| Research Abstract |
PGR3 is a PPR protein consisting of 27 PPR motifs and stabilizes the petLoperon RNA and also activates the translation of petL and ndhA. To study the function of each PPR motif, a series of mutations which inactivated the specific function of each PPR motif was introduced to PGR3. The N-terminal PPR motifs of PGR3 are required for recognizing two target RNAs by the combination of different set of PPR motifs. In contrast, the C-terminal PPR motifs were essential for activating translation of petL and ndhA. The C-terminal PPR motifs bind RNA to modify its secondary structure, the process which likely recruits the translational machinery. This function of C-terminal domain of PPR proteins is probably conserved in the PPR proteins involved in RNA editing. We hypothesize that the C-terminal domains of such PPR proteins also modify the secondary structure of RNA to recruit the RNA editing enzyme to the target site.
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Research Products
(10 results)
