| Project/Area Number |
04304055
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Yamanashi Medical University |
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Principal Investigator |
TSURUGI Kunio Yamanashi Medical University Proffesor, 医学部, 教授 (10018690)
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| Co-Investigator(Kenkyū-buntansha) |
UCHIUMI Toshio Niigata University School of Medicine Research Assistant, 医学部, 助手 (50143764)
WADA Akira Kyoto University, Faculty of Science Research Assistant, 理学部, 助手 (80025387)
TANAKA Tatsuo University of the Ryukyus, School of Medicine, Proffesor, 医学部, 教授 (70018688)
OTAKA Eiko Hiroshima University Research Institute for Nuclear Medicine and Biology, Proffe, 原医研, 教授 (30034630)
TAKAGI Masamichi University of Tokyo, Faculty of Agriculture, Proffesor, 農学部, 教授 (50018339)
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| Project Period (FY) |
1992 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥13,000,000 (Direct Cost: ¥13,000,000)
Fiscal Year 1994: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1993: ¥5,000,000 (Direct Cost: ¥5,000,000)
Fiscal Year 1992: ¥5,000,000 (Direct Cost: ¥5,000,000)
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| Keywords | Eukaryotic cell / Ribosomal proteins / Cycloheximide / Gene cloning / Evolution / 2-D PAGE / Acidic ribosomal proteins |
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| Research Abstract |
Some yeasts possese a inducible cycloheximide(CYH)-resistant ribosome and the gene resiponsible to this has been isolated which encoded one of two genes of the ribosomal protein L41. The two L41 genes are different in a substitution of the 58th glutamine codon for the proline codon and the one containing glutamine was responsible for CYH-resistance. The nucleotide sequences responsible for the inducibility by addition of CYH were found in the promoter regions which contained GT-rich and Gcn4p binding sequences.
Eukaryotic cells possess a family of acidic ribosomal proteins and the members contained evolutionarily conserved hydrophobic zippers and hydrophobic hook-and-eye struc-tures in the amino-terminal half, which are assumed to be involved in their association. They formed complex including L12 and located in the highly conserved "GTPase domain" as-sociating with a unique internal loop comprised by 1867-1914 residues of 28S rRNA.
Radical-free and highly reducing (RFHR) 2-D gel electrophoresis was developed which enabled us to clearly and reproducibly separate ribosomal proteins. With this method four new ribosomal proteins (A,B,C and D) were found in E.coli ribosome and one (SCS28) were in plant chloroplast ribosomes. Ribosomal proteins of yeast and rat liver ribosomes were also re-analyzed to determine precise number of the proteins.
Several genes for ribosomal proteins were isolated from chicken liver (L5, L7a, L30 and L37a) and yeast (YL16 and YL8), and their amino acid sequences were deduced from the nucleotide sequences. Including these proteins, equivalents among ribosomal proeins from various organism were systematically compiled using a universal code system(UCS). From the analysis an evolutionary profile of ribosomal proteins was proposed.
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