RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase (Trm8-Trm82 complex).
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.
Matsumoto
Keisuke
K
Department of Applied Chemistry, Faculty of Engineering, Ehime University, Bunkyo 3, Matsuyama 790-8577, Japan.
Toyooka
Takashi
T
Tomikawa
Chie
C
Ochi
Anna
A
Takano
Yoshitaka
Y
Takayanagi
Naoyuki
N
Endo
Yaeta
Y
Hori
Hiroyuki
H
D001665:Binding Sites; D009690:Nucleic Acid Conformation; D012360:RNA, Transfer, Phe / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D012359:tRNA Methyltransferases / Q000737:chemistry*
D012360:RNA, Transfer, Phe; D029701:Saccharomyces cerevisiae Proteins; D012359:tRNA Methyltransferases; C036814:tRNA (guanine-N7-)-methyltransferase