Aquifex aeolicus tRNA ( N 2 , N 2 - Guanine ) - dimethyltransferase ( Trm 1 ) Catalyzes Transfer of Methyl Groups Not Only to
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چکیده
Takako Awai, Satoshi Kimura, Chie Tomikawa, Anna Ochi, Ihsanawati, Yoshitaka Bessho , Shigeyuki Yokoyama **, Satoshi Ohno, Kazuya Nishikawa, Takashi Yokogawa, Tsutomu Suzuki, and Hiroyuki Hori From the Department of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo 3, Matsuyama, Ehime 790-8577, the Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-8656, the Systems and Structural Biology Center, Yokohama Institute, RIKEN, Suehiro-cho 1-7-22, Tsurumi-ku, Yokohama, Kanagawa 230-0045, the RIKEN SPring-8 Center, Harima Institute, Kouto 1-1-1, Sayo, Hyogo 679-5148, the **Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, the Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu, Gifu 501-1193, and the Venture Business Laboratory, Ehime University, Bunkyo 3, Matsuyama, Ehime 790-8577, Japan
منابع مشابه
Aquifex aeolicus tRNA (Gm18) methyltransferase has unique substrate specificity. TRNA recognition mechanism of the enzyme.
Transfer RNA (guanosine-2')-methyltransferase (Gm-methylase) catalyzes the transfer of a methyl group from S-adenosyl-l-methionine to 2'-OH of G18 in the D-loop of tRNA. Based on their mode of tRNA recognition, Gm-methylases can be divided into the following two types: type I having broad specificity toward the substrate tRNA, and type II that methylates only limited tRNA species. Protein synth...
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The editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for the faithful protein synthesis by correcting misactivated amino acids and misaminoacylated tRNAs. We report that the isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus (alphabeta-LeuRS) catalyzes the hydrolytic editing of both mischarged tRNA(Leu) and minihelix(Leu). Wit...
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Aquifex aeolicus alphabeta-LeuRS is the only known heterodimeric LeuRS, while Escherichia coli LeuRS is a canonical monomeric enzyme. By using the genes encoding A. aeolicus and E. coli LeuRS as PCR templates, the genes encoding the alpha and beta subunits from A. aeolicus alphabeta-LeuRS and the equivalent amino- and carboxy-terminal parts of E. coli LeuRS (identified as alpha' and beta') were...
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Genes to Cells (2006) 11 , 1353–1365 Journal compilation © 2006 by the Molecular Biology Society of Japan/Blackwell Publishing Ltd. 1353 DOI: 10.1111/j.1365-2443.2006.01022.x Blackwell Publishing Inc M lden, USA GTC enes to Cells 1356-9597 © Blackwell Publ shing Ltd ? 2006 1 Original Artic e tRNA specificity of Aquifex aeolicus TrmD H. Takeda e al. The substrate specificity of tRNA (m 1 G37) me...
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N(2)-guanine methyltransferase II was purified from rat liver. This enzyme methylated bulk E. coli tRNA to an extent of 7.6 nmoles of methyl groups/mg tRNA. Oligonucleotide analysis showed that N(2)-methylated guanosines were present in the modified tRNA in two sequences, namely Y-m(2)G-Cp and Y-m(2) (2)G-Cp in the ratio 4:3. Two pure tRNA(Leu) species, and tRNA(Met) (f) from E. coli were methy...
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