Nucleotide sequence of tRNA<sup>Arg</sup><sub>II</sub> from brewer's yeast

Weissenbach, Jean; Martin, Robert P.; Dirheimer, G.

doi:10.1016/0014-5793(72)80748-8

Cited by 54 publications

(7 citation statements)

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“…It is shown in the accompanying paper that methylation does indeed take place at these sites (Pegg, 1974). Conversely, tRNA"¢t and tRNAA'r (Simsek & Rajbhandary, 1972;Weissenbach et al, 1972) do not have suitable residues for methylation at these positions and these tRNA species were not substrates for methylation by enzymes from normal colon or colon tumours. These observations suggest that methylation in vitro of tRNA of micro-organisms by heterologous enzymes from mammalian cells may provide meaningful studies of the activities of these enzymes in vivo even though the substrate is unnatural.…”

Section: Discussionmentioning

confidence: 99%

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

Pegg

Hawks

1974

Biochemical Journal

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1. Extracts prepared from tumours of the mouse colon induced by 1,2-dimethylhydrazine were considerably more active in catalysing the methylation of tRNA than were extracts from normal colon. The enhanced activity was observed when both unfractionated ;methyl-deficient' tRNA and purified tRNA preparations from yeast and bacteria were used as substrates for methylation. 2. The methylated bases produced in these reactions were identified. There were no differences between the products of the reaction catalysed by extracts of tumour and normal colon. 3. The increased activity of tRNA methylases was not due to the presence in the extracts of stimulatory or inhibitory molecules of low molecular weight such as polyamines or S-adenosylhomocysteine. 4. Other enzymes concerned with tRNA metabolism (RNA polymerase, ATP-tRNA adenylyltransferase, aminoacyl-tRNA ligases) were also increased in activity in the tumour tissue. 5. The extent of methylation of a limiting amount of tRNA was greater when tumour extracts were compared with controls, but in no case was it possible to achieve a stoicheiometric methylation of the purified tRNA preparations used as substrates, and the tumour extracts were not able to methylate tRNA obtained from normal mouse colon. We conclude that the tumours contained greater activities of tRNA methylases but that there was no evidence for changes in the specificity of these enzymes during neoplastic growth.

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Section: Discussionmentioning

confidence: 99%

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

Pegg

Hawks

1974

Biochemical Journal

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Section: Discussionmentioning

confidence: 99%

“…Most of the structural features have been described in a preliminary report [5]. The comparison of the structures of brewers' yeast tRNAEg and of t R N A 2 , also sequenced in our laboratory, has been published recently [5,3]. It should be noticed that t R N A p has almost as many similarities with tRNALyS from bakers' yeast [6] or with tRNALyS from haplo'id yeast [7], ( i e .…”

Section: Discussionmentioning

confidence: 99%

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The Primary Structure of tRNAIIArg from Brewers' Yeast. 2. Partial Digestion with Ribonuclease T1 and Derivation of the Complete Sequence

1975

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Several large oligonucleotides obtained by partial digestion of tRNAFg from brewers' yeast with ribonuclease T, have been isolated and their sequences have been established. These results and those described in the preceding paper permitted the derivation of the complete primary structure of this tRNA.Larger fragments than those obtained after complete pancreatic and T, ribonucleases digestions of tRNAEg had to be obtained in order to derive the complete sequence of this tRNA. These large fragments have been produced by partial digestion with T, ribonuclease. This paper reports the conditions of controlled cleavage of tRNA;\;p with RNase TI, the separations and the analyses of the fragments obtained and the derivation of the complete primary structure of this tRNA. MATERIALS AND METHODS General MethodsSource of tRNA? and of the various enzymes, thin-layer chromatography and high-voltage electrophoresis conditions, methods of analysis and of identification of oligonucleotides and other general techniques have been described elsewhere [l -31. Polyacrylamide Gel ElectrophoresisThe action of T, ribonuclease was followed by polyacrylamide gel electrophoresis of the digests. The gels were scanned at 254 nm using a Vernon photoAbbreviations for polynucleotides follow the recommendations of IUPAC-IUB Commission on Biochemical Nomenclature for abbreviations and symbols for nucleic acids, polynucleotides and their constituents see Eur. J. Biochem. 15, 203 (1970).Definirion. A260 unit, amount of material in 1 ml of solution which gives an absorbance of 1 at 260 nm in a I-cm light path.Enzymes. Ribonuclease TI (EC 3.1.4.8); alkaline phosphatase (EC 3.1.3.1).densitometer. The optimal partial hydrolysis conditions concerning enzyme and magnesium concentrations and digesting time were determinated from the electrophoretic patterns.Partial Digestion of tRNA? with Ribonuclease T, 300 A260 units of purified tRNAEg were incubated with 200 units of RNase T1 in 12 ml of a 0.05 M Tris-HC1 buffer (pH 7.5) 0.02 M Mg C12 for 30 min at 0 "C.Enzyme was then removed by treating twice with an equal volume of phenol saturated at 0 "C with 0.05 M Tris-HC1 buffer (pH 7.5) containing 0.02 M Mg C12. The phenol phases were pooled and backextracted twice with half a volume of water. The pooled aqueous fractions were washed four times with two volumes of ethyl ether. This solution, brought to a 7 M urea concentration by addition of solid urea, was loaded on a DEAE-cellulose 7 M urea column. Separation of Large OligonucleotidesThe T, partial digest was first submitted to DEAEcellulose-7 M urea-Tris-HC1 0.02 M (pH 7.3) column chromatography (Fig. 1). Each peak of oligonucleotides isolated from the DEAE-cellulose column at pH 7.3 was diluted five-fold with 7 M urea and loaded on an other DEAE-cellulose column. This column was then equilibrated with 7 M urea-HC1, pH 3, and eluted by a linear sodium chloride gradient. Urea and salt were removed from the pooled oligonucleotide fractions as previously described [l -31.Eur. J. Biochem. 56 (1975)

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“…The DNA fragment from pY41 contains a tRNAArg gene which, in its structural part, is colinear with the RNA sequence as determined by Weissenbach et al (1972); no intron is found. The tRNAPxg gene of pY41 occurs as a single transcription unit, in contrast to a tRNAArg gene, which is arranged in a dimeric transcriptional unit together with a tRNAAsP gene in yeast (Beckman et al, 1979).…”

Section: Analysis Of the Dna Sequences From P Y44 P Y41 And P Y7mentioning

confidence: 99%

Nucleotide sequences of yeast genes for tRNA^Ser ₂ , tRNA^Arg ₂ and tRNA^Val ₁ : homology blocks occur in the vicinity of different tRNA genes

Baker¹,

Eigel²,

Vögtel³

et al. 1982

The EMBO Journal

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Three members of a collection of pBR322‐yeast DNA recombinant plasmids containing yeast tRNA genes have been analyzed and sequenced. Each plasmid carries a single tRNA gene: pY44, tRNASer2; pY41, tRNAArg2; pY7, tRNAVal1. All three genes are intronless and terminate in a cluster of Ts in the non‐coding strand. The sequence information here and previously determined sequences allow an extensive comparison of the regions flanking several yeast tRNA genes. This analysis has revealed novel features in tRNA gene arrangement. Blocks of homology in the flanking regions were found between the tRNA genes of an isoacceptor family but, more interestingly, also between genes coding for tRNAs of different amino‐acid specificities. Particularly, three examples are discussed in which sequence elements in the neighborhood of different tRNA genes have been conserved to a high degree and over long distances.

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Nucleotide sequence of tRNA^Arg_II from brewer's yeast

Cited by 54 publications

References 20 publications

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

The Primary Structure of tRNAIIArg from Brewers' Yeast. 2. Partial Digestion with Ribonuclease T1 and Derivation of the Complete Sequence

Nucleotide sequences of yeast genes for tRNA^Ser ₂ , tRNA^Arg ₂ and tRNA^Val ₁ : homology blocks occur in the vicinity of different tRNA genes

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Nucleotide sequence of tRNAArgII from brewer's yeast

Cited by 54 publications

References 20 publications

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

Further investigation of the increased transfer ribonucleic acid methylase activity in tumours of the mouse colon

The Primary Structure of tRNAIIArg from Brewers' Yeast. 2. Partial Digestion with Ribonuclease T1 and Derivation of the Complete Sequence

Nucleotide sequences of yeast genes for tRNASer 2 , tRNAArg 2 and tRNAVal 1 : homology blocks occur in the vicinity of different tRNA genes

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Nucleotide sequence of tRNA^Arg_II from brewer's yeast

Nucleotide sequences of yeast genes for tRNA^Ser ₂ , tRNA^Arg ₂ and tRNA^Val ₁ : homology blocks occur in the vicinity of different tRNA genes