Molecular switch mechanism for stop codon versatility by release factors (RF)

• Project/Area Number: 22310134
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Living organism molecular science
• Research Institution: The University of Tokyo
• Principal Investigator: ITO Koichi 東京大学, 大学院・新領域創成科学研究科, 教授 (10262073)
• Project Period (FY): 2010 – 2012
• Project Status: Completed (Fiscal Year 2012)
• Budget Amount: ¥19,630,000 (Direct Cost: ¥15,100,000、Indirect Cost: ¥4,530,000); Fiscal Year 2012: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000); Fiscal Year 2011: ¥7,540,000 (Direct Cost: ¥5,800,000、Indirect Cost: ¥1,740,000); Fiscal Year 2010: ¥7,410,000 (Direct Cost: ¥5,700,000、Indirect Cost: ¥1,710,000)
• Keywords: 翻訳終結 / リボソーム / tRNA / 分子擬態 / ペプチド鎖解離因子 / 遺伝暗号解読 / タンパク質合成 / ペプチド鎖解離因

Research Abstract

Here we solved the first crystal structure of aRF1 and aPelota from an archaeon, Aeropyrum pernix (ape-aRF1) complexed with archaeal translation elongation factor aEF1α. Our biochemical and genetic analyses revealed that the authentic archaeal EF1α acts as a carrier GTPase for aRF1, and surprisingly, for aPelota, which functions in the mRNA surveillance pathways via tRNA mimicry. Our results revealed novel aspects of GTP switch mechanism for stop codon recognition.

Research Products

• [Journal Article] A Single Amino Acid Substitution Alters Omnipotent eRF1 of Dileptus to Euplotes-type Dualpotent eRF1 (2013)
  • Author(s): Li Y, Kim OT, Ito K, Saito K, Suzaki T,Harumoto T.
  • Journal Title: Standard Codon Usage May be Advantageous in Raptorial Ciliates. Protist. Volume: 164 Issue: 3 Pages: 440-449
  • DOI: 10.1016/j.protis.2013.02.004
  • Peer Reviewed
• [Journal Article] Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex. (2012)
  • Author(s): Kan Kobayashi, Kazuki Saito, Ryuichiro Ishitani, Koichi Ito, Osamu Nureki
  • Journal Title: Nucleic Acids Res. Volume: 40 Issue: 18 Pages: 9319-9328
  • DOI: 10.1093/nar/gks660
  • Peer Reviewed
• [Journal Article] Single molecule imaging of the trans-translation entry process via anch oring of the tagged ribosome. (2011)
  • Author(s): Zhou, Z-P., Shimizu, Y., Tadakuma, H.*, Taguchi, H., Ito, K., Ueda, T.
  • Journal Title: J. Biochem. Volume: 149 Issue: 5 Pages: 609-618
  • DOI: 10.1093/jb/mvr010
  • NAID: 10030585460
  • Peer Reviewed
• [Journal Article] tRNA mimicry in translation termination and beyond. (2011)
  • Author(s): Nakamura, Y., Ito, K.
  • Journal Title: Wiley Interdiscip Rev (WIREs) RNA. Volume: 2 Issue: 5 Pages: 647-668
  • DOI: 10.1002/wrna.81
  • Peer Reviewed
• [Journal Article] Stmctural Basis for mRNA Surveillance by Archaeal Pelota and GTP-bound EF1α Complex (2010)
  • Author(s): Kobayashi, K. Kikuno,1. Kuroha, K. Saito, K. Ito, K. Ishitani, R. Inada. T. and Nureki, O
  • Journal Title: Proc. Natl. Acad. Sci. USA Volume: 107 Issue: 41 Pages: 17575-17579
  • DOI: 10.1073/pnas.1009598107
  • Peer Reviewed
• [Journal Article] An omnipotent role of archaeal EF1α in translational elongation and termination, and quality control of protein synthesis. (2010)
  • Author(s): Saito K, Kobayashi K, Wada M, Kikuno I, Takusagawa A, Mochizuki M, Uchiumi T, Ishitani R, Nureki O and Ito K
  • Journal Title: Proc Natl Acad Sci USA Volume: 107 Issue: 45 Pages: 17575-17579
  • DOI: 10.1073/pnas.1009599107
  • Peer Reviewed
• [Journal Article] An omnipotent role of archaeal EF1α in translational elongation and termination, and quality control of protein synthesis. (2010)
  • Author(s): Saito K
  • Journal Title: Proc.Natl.Acad.Sci.USA Volume: 107 Pages: 19242-19247
  • Peer Reviewed
• [Journal Article] Structural Basis for mRNA Surveillance by Archaeal Pelota and GTP-bound EF1α Comolex. (2010)
  • Author(s): Kobayashi K
  • Journal Title: Proc.Natl.Acad.Sci.USA Volume: 107 Pages: 17575-17579
  • Peer Reviewed
• [Presentation] Analysis of stop codon decoding in eukaryotes. (2012)
  • Author(s): Saito K., Ito K.
  • Organizer: 第35回日本分子生物学会年会
  • Place of Presentation: 福岡、福岡国際会議場、マリンメッセ福岡
• [Presentation] 3 'to 5' mRNA degradation activating factor SKI7 contains a conserved functional motif in its N- terminal domain. (2012)
  • Author(s): Saito K., Ito K.
  • Organizer: 第35回日本分子生物学会年会
  • Place of Presentation: 福岡、福岡国際会議場、マリンメッセ福岡
• [Presentation] Structural basis for translation termination by archaeal RF1 and GTP- bound EF1α complex (2012)
  • Author(s): Kan Kobayashi, Kazuki Saito, Ryuichiro Ishitani, Koichi Ito, and Osamu Nureki
  • Organizer: XXIV tRNA Conference
  • Place of Presentation: Chile
• [Presentation] Structural basis for mRNA surveillance by Archaeal Pelota and GTP- bound EF1alpha complex (2012)
  • Author(s): Ryuichiro Ishitani, Kan Kobayashi, Izumi Kikuno, Kazushige Kuroha, Kazuki Saito, Koichi Ito, Toshifumi Inada, and Osamu Nureki
  • Organizer: XXIV tRNA Conference
  • Place of Presentation: Chile
• [Presentation] 3'to5' mRNA degradation activating factor SKI7 contains a conserved functional motif in its N-terminal domain. (2012)
  • Author(s): Horikawa W., Wada M., Ito K.
  • Organizer: 第35回日本分子生物学会年会
  • Place of Presentation: 福岡、福岡国際会議場、マリンメッセ福岡
• [Presentation] Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex (2012)
  • Author(s): Kan Kobayashi, Kazuki Saito, Ryuichiro Ishitani, Koichi Ito, and Osamu Nureki,
  • Organizer: XXIV tRNA Conference
  • Place of Presentation: Olmué, Chile.
• [Presentation] Structural basis for mRNA surveillance by Archaeal Pelota and GTP-bound EF1alpha complex (2012)
  • Author(s): (7) Ryuichiro Ishitani, Kan Kobayashi, Izumi Kikuno, Kazushige Kuroha, Kazuki Saito, Koichi Ito, Toshifumi Inada, and Osamu Nureki
  • Organizer: XXIV tRNA Conference
  • Place of Presentation: Olmué, Chile.
• [Presentation] Structural Basis for Translation Termination by Archaeal RF1 and GTP-bound EF1α Complex (2011)
  • Author(s): Kan Kobayashi, Kazuki Saito, Ryuichiro Ishitani, Koichi Ito, Osamu Nureki
  • Organizer: The 16th Annual Meeting of The RNA Society
  • Place of Presentation: Kyoto, Kyoto International Conference Center
• [Presentation] Omnipotent Role of Archaeal Elongation Factor 1 Alpha in Translation Elongation, and Termination, and Quality Control of Protein Synthesis (2011)
  • Author(s): Kazuki Saito, Kan Kobayashi, Miki Wada,Izumi Kikuno, Akira Takusagawa, Masahiro Mochizuki, Toshio Uchiumi, Ryuichiro Ishitani,Osamu Nureki, Koichi Ito
  • Organizer: The 16th Annual Meeting of The RNA Society
  • Place of Presentation: Kyoto, Kyoto International Conference Center
• [Presentation] Archaeal elongation factor acts as an omnipotent carrier GTPase in translational elongation, termination and mRNA surveillance (2011)
  • Author(s): Osamu Nureki1, Kan Kobayashi1, Kazuki Saito, Toshio Uchiumi, Ryuichiro Ishitani, Toshifumi Inada, koichi ito
  • Organizer: The 16th Annual Meeting of The RNA Society
  • Place of Presentation: Kyoto, Kyoto International Conference Center
• [Presentation] A Translational Fine-tuning by The Drg2-GTPase/Dfrp2 Complex (2011)
  • Author(s): Kosuke Ishikawa, Koichi Ito, Kentaro Semba
  • Organizer: The 16th Annual Meeting of The RNA Society
  • Place of Presentation: Kyoto, Kyoto International Conference Center
• [Presentation] Genetic Analyses of Critical Sites for eRF1-eRF3 Interplay in Translation Termination (2011)
  • Author(s): Wada M, Nakamura Y, Ito K
  • Organizer: The 16th Annual Meeting of The RNA Society
  • Place of Presentation: Kyoto, Kyoto International Conference Center
• [Presentation] Establishment of a novel dual luciferase reporter assay for No-go decay mRNA quality control. (2011)
  • Author(s): Horikawa W, Ito K
  • Organizer: 日本分子生物学会年会
  • Place of Presentation: 横浜、パシフィコ横浜
• [Presentation] 真核生物型翻訳終結機構とGタンパク質分子機構の普遍性 (2010)
  • Author(s): 伊藤耕一
  • Organizer: 第33回日本分子生物学会年会
  • Place of Presentation: 神戸
  • Year and Date: 2010-12-07
• [Presentation] 真核生物型翻訳終結機構とGタンパク質分子機構の普遍性 (2010)
  • Author(s): 伊藤耕一
  • Organizer: 第33回日本分子生物学会年会
  • Place of Presentation: 神戸国際展示場
  • Year and Date: 2010-12-07
• [Remarks]
  • URL: http://www.k.u-tokyo.ac.jp/mgs/mgs_info/molgenet/research.html