| Literature DB >> 17382321 |
Keisuke Matsumoto1, Takashi Toyooka, Chie Tomikawa, Anna Ochi, Yoshitaka Takano, Naoyuki Takayanagi, Yaeta Endo, Hiroyuki Hori.
Abstract
Yeast tRNA (m(7)G46) methyltransferase contains two protein subunits (Trm8 and Trm82). To address the RNA recognition mechanism of the Trm8-Trm82 complex, we investigated methyl acceptance activities of eight truncated yeast tRNA(Phe) transcripts. Both the D-stem and T-stem structures were required for efficient methyl-transfer. To clarify the role of the D-stem structure, we tested four mutant transcripts, in which tertiary base pairs were disrupted. The tertiary base pairs were important but not essential for the methyl-transfer to yeast tRNA(Phe) transcript, suggesting that these base pairs support the induced fit of the G46 base into the catalytic pocket.Entities:
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Year: 2007 PMID： 17382321 DOI： 10.1016/j.febslet.2007.03.023
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124