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Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27.

Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Research Abstract Details 

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  • Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Abstract Text:

    t matsumotoT Matsumoto,k nishikawaK Nishikawa,h horiH Hori,t ohtaT Ohta,k miuraK Miura,k watanabeK Watanabe,

    Recognition sites of tRNA by tRNA(guanosine-2'-)-methyltransferase (Gm-methylase) [EC 2.1.1.34] from an extreme thermophile, Thermus thermophilus HB27, were studied by two independent methods--fragment reactions and footprinting analyses, using yeast tRNA(Phe) and Escherichia coli tRNA(fMet) as substrates. None of the tRNA-derived oligonucleotides which have the G-G sequence but are not long enough to form the "stem-loop" structure could be methylated by Gm-methylase. The 5'-half fragments having the intact D-"stem-loop" structure served as substrates for Gm-methylase, with a similar Vmax but 6-8 times larger Km, as compared with the intact tRNAs. The results of footprinting analyses were consistent with the foregoing findings. Gm-methylase protected only the D-loop region of tRNA from RNase T1 attack, but other parts of tRNA extending from the amino acid stem to the T arm became more sensitive to RNase T1, suggesting a considerable change of tRNA tertiary structure due to complex formation with Gm-methylase. These results indicate that a D-"stem-loop" structure is a prerequisite for recognition by Gm-methylase.

    Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Publishing Authors By Initials

    t matsumotoT Matsumoto,k nishikawaK Nishikawa,h horiH Hori,t ohtaT Ohta,k miuraK Miura,k watanabeK Watanabe,

    For similar enzymes and coenzymes: enzymes: transferases: one-carbon group transferases: methyltransferases: trna methyltransferases research abstracts see: enzymes and coenzymes: enzymes: transferases: one-carbon group transferases: methyltransferases: trna methyltransferases research

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    Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 107

    Page Numbers: 331-8

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Mar

    YEAR: 1990

    Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Keywords Mesh Terms:

    KEYWORDS: tRNA Methyltransferases

    MESH TERMS: genetics

    Chemical & Substance for Abstract: Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. Information

    Substance Name: Ribonucleases

    Registry Number: EC 3.1.-

    Grant and Affiliation Information for Recognition sites of tRNA by a thermostable tRNA(guanosine-2'-)-methyltransferase from Thermus thermophilus HB27.

    AFFILIATION: Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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