Purification and characterization of tRNA(adenosine-1-)-methyltransferase from Thermus thermophilus HB27.

N. Yamazaki, H. Hori, K. Ozawa, S. Nakanishi, Takuya Ueda, I. Kumagai, K. Watanabe, K. Nishikawa

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Abstract

A58, the conserved adenosine residue in the T psi C loop of tRNAs, is methylated to m1A 58 in an extreme thermophile, Thermus thermophilus HB27. The enzyme catalyzing this methyltransfer reaction was purified from the thermophle. The substrate specificity of the enzyme was investigated by using tRNA fragments. The enzyme can transfer the methyl group to the 3'-half fragment of E. coli initiator tRNA, indicating that the main recognition site of the enzyme exists in the 3' half of tRNA including the T-loop and the T-stem.

Original languageEnglish
Pages (from-to)141-142
Number of pages2
JournalNucleic acids symposium series
Issue number27
Publication statusPublished - 1992 Jan 1
Externally publishedYes

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ASJC Scopus subject areas

  • Medicine(all)

Cite this

Yamazaki, N., Hori, H., Ozawa, K., Nakanishi, S., Ueda, T., Kumagai, I., Watanabe, K., & Nishikawa, K. (1992). Purification and characterization of tRNA(adenosine-1-)-methyltransferase from Thermus thermophilus HB27. Nucleic acids symposium series, (27), 141-142.