Recognition mechanism of tRNA with tRNA(guanosine-2')methyltransferase from Thermus thermophilus HB 27.
rRNA(Gm)methyltransferase from an extreme thermophile, Thermus thermophilus HB 27 specifically methylates the 2'-OH of the ribose ring of G18 in the invariant G18-G19 sequence in the D loop of tRNA. The interaction site on tRNA was presumed to be the D loop and stem structure. Destruction of tertiary structure of tRNA caused by heat resulted in a great decrease in the acceptor activity of methyl group. It was suggested by CD measurement that a conformational change of tRNA occurs when it forms an equimolar complex with Gm-methylase.
D001483:Base Sequence; D007700:Kinetics; D009690:Nucleic Acid Conformation; D012343:RNA, Transfer / Q000378:metabolism*; D013379:Substrate Specificity; D013816:Thermodynamics; D013824:Thermus / Q000201:enzymology*; D012359:tRNA Methyltransferases / Q000378:metabolism*
D012343:RNA, Transfer; D012359:tRNA Methyltransferases; C023196:tRNA (guanine(10)-N(2))-dimethyltransferase