In Vivo Function of tRNase Z in Esherichia coli and Yeast Saccharomyces cerevisiae
| Project/Area Number |
20780063
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied microbiology
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| Research Institution | Nigata University of Phermacy and Applied Life Sciences |
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Principal Investigator |
TAKAKU Hiroaki Nigata University of Phermacy and Applied Life Sciences, 応用生命科学部, 准教授 (70350717)
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| Co-Investigator(Renkei-kenkyūsha) |
NASHIMOTO Masayuki 新潟薬科大学, 応用生命科学部, 教授 (30228069)
TAKAGI Masamichi 新潟薬科大学, 学長 (50018339)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 微生物酵素 / tRNaseZ / 前駆体tRNA / 酵母 / tRNAの3'プロセシング / エンド型リボヌクレアーゼ / tRNase Z / 成熟tRNA / 大腸菌 / アミノアシルtRNA |
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| Research Abstract |
In most organisms, tRNase Z is thought to be essential for 3′ processing of tRNA molecules. The Escherichia coli tRNase ZS gene, however, appears to be dispensable under normal growth conditions. Here we intensively examined various (pre-)tRNAs for good substrates of E. coli tRNase ZS in vitro, and found that the enzyme can nibble off the 3′ terminal CCA residues from mature tRNAs. Furthermore, we discovered that E. coli tRNase ZS, when sufficiently expressed in the cell, shuts down growth by removing amino acids from aminoacyl-tRNAs. The current data suggest that tRNase ZS may help modulate a cell growth rate by repressing translation under some stressful conditions. We also examined 3′ processing activity of recombinant yeast tRNase ZL against various yeast pre-tRNAs in vitro. The recombinant yeast tRNase ZL was able to cleavage yeast pre-tRNAs efficiently after the discriminator nucleotide. Taken together, we speculate the difference of tRNase Z domain structure between E. coli and yeast might lead to the specificity of substrate recognition and cleavage site.
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Report
(3 results)
Research Products
(2 results)
