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Nucleic Acids Symposium Series 2005 49(1):303-304; doi:10.1093/nass/49.1.303
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© 2005 Oxford University Press

Aquifex aeolicus Trm1[tRNA (m22G26) methyltransferase] has a novel recognition mechanism of the substrate RNA

Takako Awai1, Toru Takehara1, Hiroshi Takeda1 and Hiroyuki Hori1,2

1 Department of Applied Chemistry, Faculty of Engineering, Ehime University, Bunkyo 3, Matsuyama 790-8577, Japan, 2 Venture Business Laboratory, Ehime University, Matsuyama 790-8577, Japan

Aquifex aeolicus is a hyper-thermophilic eubacterium, which probably diverged at the earliest period from the other bacteria on the evolution of life. Therefore, analyses of RNA modification enzymes of this bacterium may supply important information in relation to the establishment of the early protein synthesis. In the previous meeting, we have reported that Aquifex aeolicus trm1 gene product possesses a tRNA (m22G26) methyltransferase activity. This enzyme catalyzes the methyl-transfer from S-adenosyl-L-methionine to the semi-conserved residue, G26, via the intermediate modified base, m2G26. In this meeting, we report the A. aeolicus Trm1 large scale expression system in E.coli and the substrate RNA recognition mechanism of the enzyme.


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