Recognition mechanism of tRNA with tRNA(guanosine-2')methyltransferase from Thermus thermophilus HB 27

Nucleic Acids Symp Ser. 1984:(15):131-4.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Kinetics
  • Nucleic Acid Conformation
  • RNA, Transfer / metabolism*
  • Substrate Specificity
  • Thermodynamics
  • Thermus / enzymology*
  • tRNA Methyltransferases / metabolism*

Substances

  • RNA, Transfer
  • tRNA Methyltransferases
  • tRNA (guanine(10)-N(2))-dimethyltransferase