Premium
RNA recognition mechanism of eukaryote tRNA (m 7 G46) methyltransferase (Trm8–Trm82 complex)
Author(s) -
Matsumoto Keisuke,
Toyooka Takashi,
Tomikawa Chie,
Ochi Anna,
Takano Yoshitaka,
Takayanagi Naoyuki,
Endo Yaeta,
Hori Hiroyuki
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.023
Subject(s) - transfer rna , yeast , methyltransferase , rna , eukaryote , base pair , protein tertiary structure , mutant , biology , biochemistry , genetics , chemistry , methylation , gene , genome
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.