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Differences of tRNA identity between Escherichia coli and Saccharomyces cerevisiae (yeast).

Research Project

Project/Area Number 06680633
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Functional biochemistry
Research InstitutionInstitute of Space and Astronautical Science

Principal Investigator

HASEGAWA Tsunemi  Planetary Science Division, Associate Professor, 惑星研究系, 助教授 (60095023)

Project Period (FY) 1994 – 1995
Project Status Completed (Fiscal Year 1995)
Budget Amount *help
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1995: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1994: ¥1,300,000 (Direct Cost: ¥1,300,000)
KeywordstRNA Identity / Escherichia coli / Saccharomyces cerevisiae (yeast) / Thermus thermophilus / tRNA^<Thr> / tRNA^<Gly> / T7 transcript / Evolution / アイデンティティー / アンチコドン / 識別位塩基 / トレオニル-tRNA合成酵素 / 大腸菌 / 酵母 / 高度好熱菌 / tRNA^<Pro> / アミノアシル-tRNA合成酵素 / アミノアシル化 / in vitro転写反応
Research Abstract

Correct recognition of tRNAs by their cognate aminoacy-tRNA synthetases is essential to the maintenance of accurate translation. To discriminate the cognate tRNA from a pool of various tRNA species sharing a similar L-shaped tertiary structure, the aminoacyl-tRNA synthetase was found to recognize a relatively small number of nucleotides of the tRNA,which offen include the anticodon nucleotides and the discriminator base at position 73. Most of the available data are biased to the Escherichia coli system, although a few studies in other organisms have recently been made. We examined the identity elements of several tRNA species from Saccharomyces cerevisiae (yeast) and Thermus thermophilus using in vitro transcripts. For E.coli, T.thermophilus and yeast tRNA^<Thr>, the first base pair in the acceptor stem and the second and third positions of the anticodon are indeed retained as major identity elements. However the second base pair, C2-G71, in the acceptor stem is required for aminoacylation with threonine in E.coli, but not in T.thermophilus or yeast. In addition, the discriminator base, A73, in E.coli is not involved in the specific aminoacylation, whereas U73 in T.thermophilus and A73 in yeast contribute to the tRNA identity, although with differences in the quantitative effects on mutations. In case of glycine tRNAs, discriminator base, the second base pair in the acceptor stem, and the anticodon nuclotides, C35 and C36, contribute to the specific glycylation of all three glycly-tRNA synthetases, the discriminator base differing between prokaryotes (U73) and eukaryote (A73) . The first base pair, G1-C72, is important for glycylation in E.coli and T.thermophilus, whereas the third base pair is important for glycylation in yeast. These above results indicate that while major identity elements have been conserved throughout evolution, the mechanism by which aminoacyl-tRNA synthetases recognize their substrates seems to have diverged somewhat among different species.

Report

(3 results)
  • 1995 Annual Research Report   Final Research Report Summary
  • 1994 Annual Research Report
  • Research Products

    (26 results)

All Other

All Publications (26 results)

  • [Publications] 田村 浩二: "tRNAに共通に存在するCCA末端構造の機能" Viva Origino. 24. 125-135 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Nameki, N.: "Identity elements of Thermus thermophilus tRNA^<Thr>." FEBS Letters. 396. 201-207 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Asahara, H.: "Escherichia coli seryl-tRNA synthetase recognizes tRNA^<Ser> by itscharacteristic tertiary structure." Journal of Molecular Biology. 236. 738-748 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Tamura, K.: "Role of the CCA terminal sequence of tRNA^<Val> in aminoacylation with valyl-tRNA synthetase" Journal of Biological Chemistry. 269. 22173-22177 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Tamura, K.: "Roles of the CCA end of tRNA in translational processes." Nucleic Acids Symposium Series. 31. 277-278 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Nameki, N.: "Similarities and differences in tRNA identity between Escherichia coli and Saccharomyces cerevisiae:evolutionary conservation and devergence" Nucleic Acids Symposium Series. 34. 205-206 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] 長谷川 典巳: "tRNAのアイデンティティー-大腸菌の系を中心として-" 蛋白質 核酸 酵素. 40. 1474-1484 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Asahara, H.: "In vitro selection of tRNAs aminoacylated by E. coli leucyl-tRNA synthetase" Nucleic Acids Symposium Series. 35. 281-282 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Asahara, H., Himeno, H., Tamura, K., Nameki, N., Hasegawa, T.and Shimizu, M.: "Escherichia coli seryl-tRNA synthetase recognizes tRNA^<Ser> by its characteristic tertiary structure." Journal of Molecular Biology. Vol.236, No.3. 738-748 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Tamura, K., Nameki, N., Hasegawa, T., Shimizu, M.and Himeno, H.: "Role of the CCA terminal sequende of tRNA^<Val> in aminoacylation with valyl-tRNA synthetase." Journal of Biological Chemistry. Vol.269, No.35. 22173-22177 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Tamura, K., Himeno, H., Asahara, H., Nameki, N., Hasegawa, T.and Shimizu, M.: "Roles of the CCA end of tRNA in translational processes." Nucleic Acids Symposium Series. Vol.31. 277-278 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Nameki, N., Asahara, H., Tamura, K., Himeno, H., Hasegawa, T.and Shimizu, M.: "Similarities and differences in tRNA identity between Escherichia coli and Saccharomyces cerevisiae : evolutionary conservation and devergence." Nucleic Acids Symosium Series. Vol.34. 205-206 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Hasegawa, T.: "tRNA identity-A view of Escherichia coli system. (Review, Japanese)" Tanpakushitsu Kakusan Koso. Vol.40, No.10. 1474-1484 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Asahara, H., Nameki, N.and Hasegawa, T.: "In vitro selection of tRNAs aminoacylated by E.coli leucyl-tRNA synthetase." Nucleic Acids Symposium Series. Vol.35. 281-282 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Tamura, K.and Hasegawa, T.: "Functions of the universal CCA end of tRNA in translational processes. (Review, Japanese)" Viva Origino. Vol.24, No.2. 125-135 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Nameki, N., Asahara, H.and Hasegawa, T.: "Identity elements of Thermus thermophilus tRNA^<Thr>." FEBS Letters. Vol.396, No.2/3. 201-207 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Asahara,H.: "Escherichia coli seryl-tRNA synthetase recognizes tRNA ^<Ser> by its characteristic tertiary structure." Journal of Molecular Biology. 236. 738-748 (1994)

    • Related Report
      1995 Annual Research Report
  • [Publications] Tamura,K.: "Role of the CCA terminal sequence of tRNA ^<Val> in aminoacylation with valyl-tRNA synthetase." Journal of Biological Chemistry. 269. 22173-22177 (1994)

    • Related Report
      1995 Annual Research Report
  • [Publications] Tamura,K.: "Roles of the CCA end of tRNA in translational processes." Nucleic Acids Symposium Series. 31. 277-278 (1994)

    • Related Report
      1995 Annual Research Report
  • [Publications] 長谷川典巳: "tRNAのアイデンティティー、-大腸菌の系を中心にして-" 蛋白質 核酸 酵素. 40. 1474-1484 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Nameki,N.: "Similarities and differences in tRNA identity between Escherichia coli and Saccharomyces cerevisiae : Evolutionary conservation and devergence." Nucleic Acids Symposium Series. 34. 205-206 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] 田村浩二: "tRNAに共通に存在するCCA末端構造の機能" Viva Origino. 24(印刷中). (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Asahara,H.et al.: "Escherichia coli seryl-tRNA synthetase recognizes tRNA^<Ser> by its characteistic tertiary structure." Journal of Molecular Biology. 236. 738-748 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Tamura,K.et al.: "Role of the CCA terminal sequence of tRHA^<Val> in aminoacylation with valyl-tRNA synthetase." Journal of Biological Chemistry. 269. 22173-22177 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Tamura,K et al.: "Role of the CCA end of tRNA in the traslational processes." Nucleic Acids Symposium Series. 31. 277-278 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] 長谷川典巳: "tRNAのアイデンティティー、-大腸菌の系を中心にして-" 蛋白質核酸酵素. 40(印刷中). (1995)

    • Related Report
      1994 Annual Research Report

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Published: 1994-04-01   Modified: 2016-04-21  

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