Identification of essential amino acid residues of tRNA (Gm18)methyltransferase for methyl-transfer activity.

K. Watanabe; H. Hori; Y. Endo

doi:10.1093/nass/1.1.33

Identification of essential amino acid residues of tRNA (Gm18)methyltransferase for methyl-transfer activity.

K. Watanabe, H. Hori, Y. Endo

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Abstract

Recent computation analyses have pointed out an existence of conserved amino acid motifs among RNA ribose 2'-O-methyltransferases. However, the functions of these motifs are unclear yet. We carried out the site-directed mutagenesis studies systematically on Thermus thermophilus HB8 tRNA (Gm18) methyltransferase gene. Subsequent biochemical analyses with purified variant enzymes clearly revealed that five conserved amino acid residues (Asn35, Arg41, Glu124, Ser150, and Asn152) are involved in S-adenosyl-L-methionine binding. This is for the first time reporting the function of the conserved motifs among RNA ribose 2'-O-methyltransferases.

Original language	English
Pages (from-to)	33-34
Number of pages	2
Journal	Nucleic acids research. Supplement (2001)
Issue number	1
DOIs	https://doi.org/10.1093/nass/1.1.33
Publication status	Published - 2001
Externally published	Yes

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Medicine(all)

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abstract = "Recent computation analyses have pointed out an existence of conserved amino acid motifs among RNA ribose 2'-O-methyltransferases. However, the functions of these motifs are unclear yet. We carried out the site-directed mutagenesis studies systematically on Thermus thermophilus HB8 tRNA (Gm18) methyltransferase gene. Subsequent biochemical analyses with purified variant enzymes clearly revealed that five conserved amino acid residues (Asn35, Arg41, Glu124, Ser150, and Asn152) are involved in S-adenosyl-L-methionine binding. This is for the first time reporting the function of the conserved motifs among RNA ribose 2'-O-methyltransferases.",

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AB - Recent computation analyses have pointed out an existence of conserved amino acid motifs among RNA ribose 2'-O-methyltransferases. However, the functions of these motifs are unclear yet. We carried out the site-directed mutagenesis studies systematically on Thermus thermophilus HB8 tRNA (Gm18) methyltransferase gene. Subsequent biochemical analyses with purified variant enzymes clearly revealed that five conserved amino acid residues (Asn35, Arg41, Glu124, Ser150, and Asn152) are involved in S-adenosyl-L-methionine binding. This is for the first time reporting the function of the conserved motifs among RNA ribose 2'-O-methyltransferases.

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Identification of essential amino acid residues of tRNA (Gm18)methyltransferase for methyl-transfer activity.

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