Sites of methylation of purified transfer ribonucleic acid preparations by enzymes from normal tissues and from tumours induced by dimethylnitrosamine and 1,2 dimethylhydrazine

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Abstract

The sites within the tRNA sequence of nucleosides methylated by the action of enzymes from mouse colon, rat kidney and tumors of these tissues acting on tRNA(Asp) from yeast and on tRNA2(Glu), tRNA(fMet) and tRNA1(Val) from Escherichia coli were determined. The same sites in a particular tRNA were methylated by all of these extracts. Thus tRNA2(Glu) was methylated at the cytidine residue at position 48 and the adenosine residue at position 58 from the 5' end of the molecule; tRNA(Asp) was methylated at the guanosine residue at position 26 from the 5' end of the molecule; tRNA(fMet) was methylated at the guanosine residues 9 and 27, the cytidine residue 49 and the adenosine residue 59 from the 5' end, and tRNA1(Val) was methylated at the guanosine residue 10, the cytidine residue 48 and the adenosine residue 58 from the 5' end. All of these sites within the clover leaf structure of the tRNA sequence are occupied by a methylated nucleoside in some tRNA species of known sequence. It is concluded that methylation of tRNA from micro organisms by enzymes from mammalian tissues in vitro probably does accurately represent the specificity of these enzymes in vivo. However, there was no evidence that the tumor extracts, which had considerably greater tRNA methylase activity than the normal tissues, had methylases with altered specificity capable of methylating sites not methylated in the normal tissues.

Original languageEnglish (US)
Pages (from-to)239-248
Number of pages10
JournalBiochemical Journal
Volume137
Issue number2
DOIs
StatePublished - Jan 1 1974

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1,2-Dimethylhydrazine
Dimethylnitrosamine
Methylation
Transfer RNA
Tumors
Tissue
Cytidine
Guanosine
RNA, Transfer, Asp
Enzymes
Adenosine
Neoplasms
Nucleosides
Medicago
Molecules
Yeast
Escherichia coli
Rats
Colon
Yeasts

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Sites of methylation of purified transfer ribonucleic acid preparations by enzymes from normal tissues and from tumours induced by dimethylnitrosamine and 1,2 dimethylhydrazine",
abstract = "The sites within the tRNA sequence of nucleosides methylated by the action of enzymes from mouse colon, rat kidney and tumors of these tissues acting on tRNA(Asp) from yeast and on tRNA2(Glu), tRNA(fMet) and tRNA1(Val) from Escherichia coli were determined. The same sites in a particular tRNA were methylated by all of these extracts. Thus tRNA2(Glu) was methylated at the cytidine residue at position 48 and the adenosine residue at position 58 from the 5' end of the molecule; tRNA(Asp) was methylated at the guanosine residue at position 26 from the 5' end of the molecule; tRNA(fMet) was methylated at the guanosine residues 9 and 27, the cytidine residue 49 and the adenosine residue 59 from the 5' end, and tRNA1(Val) was methylated at the guanosine residue 10, the cytidine residue 48 and the adenosine residue 58 from the 5' end. All of these sites within the clover leaf structure of the tRNA sequence are occupied by a methylated nucleoside in some tRNA species of known sequence. It is concluded that methylation of tRNA from micro organisms by enzymes from mammalian tissues in vitro probably does accurately represent the specificity of these enzymes in vivo. However, there was no evidence that the tumor extracts, which had considerably greater tRNA methylase activity than the normal tissues, had methylases with altered specificity capable of methylating sites not methylated in the normal tissues.",
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N2 - The sites within the tRNA sequence of nucleosides methylated by the action of enzymes from mouse colon, rat kidney and tumors of these tissues acting on tRNA(Asp) from yeast and on tRNA2(Glu), tRNA(fMet) and tRNA1(Val) from Escherichia coli were determined. The same sites in a particular tRNA were methylated by all of these extracts. Thus tRNA2(Glu) was methylated at the cytidine residue at position 48 and the adenosine residue at position 58 from the 5' end of the molecule; tRNA(Asp) was methylated at the guanosine residue at position 26 from the 5' end of the molecule; tRNA(fMet) was methylated at the guanosine residues 9 and 27, the cytidine residue 49 and the adenosine residue 59 from the 5' end, and tRNA1(Val) was methylated at the guanosine residue 10, the cytidine residue 48 and the adenosine residue 58 from the 5' end. All of these sites within the clover leaf structure of the tRNA sequence are occupied by a methylated nucleoside in some tRNA species of known sequence. It is concluded that methylation of tRNA from micro organisms by enzymes from mammalian tissues in vitro probably does accurately represent the specificity of these enzymes in vivo. However, there was no evidence that the tumor extracts, which had considerably greater tRNA methylase activity than the normal tissues, had methylases with altered specificity capable of methylating sites not methylated in the normal tissues.

AB - The sites within the tRNA sequence of nucleosides methylated by the action of enzymes from mouse colon, rat kidney and tumors of these tissues acting on tRNA(Asp) from yeast and on tRNA2(Glu), tRNA(fMet) and tRNA1(Val) from Escherichia coli were determined. The same sites in a particular tRNA were methylated by all of these extracts. Thus tRNA2(Glu) was methylated at the cytidine residue at position 48 and the adenosine residue at position 58 from the 5' end of the molecule; tRNA(Asp) was methylated at the guanosine residue at position 26 from the 5' end of the molecule; tRNA(fMet) was methylated at the guanosine residues 9 and 27, the cytidine residue 49 and the adenosine residue 59 from the 5' end, and tRNA1(Val) was methylated at the guanosine residue 10, the cytidine residue 48 and the adenosine residue 58 from the 5' end. All of these sites within the clover leaf structure of the tRNA sequence are occupied by a methylated nucleoside in some tRNA species of known sequence. It is concluded that methylation of tRNA from micro organisms by enzymes from mammalian tissues in vitro probably does accurately represent the specificity of these enzymes in vivo. However, there was no evidence that the tumor extracts, which had considerably greater tRNA methylase activity than the normal tissues, had methylases with altered specificity capable of methylating sites not methylated in the normal tissues.

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