Chromatographic and functional comparison of human placenta and HeLa cell tyrosine transfer ribonucleic acids

Olsen, Charles E.; Penhoet, Edward E.

doi:10.1021/bi00666a016

Cited by 11 publications

(5 citation statements)

References 19 publications

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“…The codon.-depen.dent ribosome binding ability of the late-eluting tRNAAsp and an earlier eluting tRNAAsp were compared and found to be approximately the same. If the late-eluting peak in these studieA [21,22] is identical to our wobble-guanosine containing late-eluting peak, it would therefore seem that the function. of these tRNAs in protein synthesis associated reaction.s is independent of the Q modification in.…”

Section: Resultsmentioning

confidence: 63%

“…A recent report by Olsen. and Penhoet [22] describing comparative studies of tRNATyr from human. placenta an.d HeLa cells indicates that no significant differences exist in.…”

Section: Resultsmentioning

confidence: 99%

“…contrast to the results obtained with the various mammalian. tRNA Asp [21] an.d the HeLa cell tRNA2yr [22]. Therefore, at present it seems that in protein synthesis the role of these Q (and Q*) or guan.osine might play an.…”

Section: Resultsmentioning

confidence: 99%

“…The earlier work in this area has been reviewed [7] and more recent reports of alterations in. tRNA chromatographic mobility have been published [5,[8][9][10][11][12][13][14][15][16][17][18][19][20][21][22]. Only in a few instances [5,[8][9][10][11][12][13] has the specific alteration, been investigated fully enough to identify the structural change which caused the observed chromatographic shift in.…”

Section: C) Information Retrieval Limited 1 Falconberg Court London Wmentioning

confidence: 99%

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Comparison of rat liver and Walker 256 carcinosarcoma tRNAs

et al. 1979

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The complete nucleotide sequences of both rat liver and Walker 256 mammary carcinosarcoma tRNAAsn reveal that they are identical except for the nucleotide present in the wobble position of the anticodon loop. The rat liver tRNAAsn contains the Q nucleoside, whereas the tumour tRNAAsn contains an unmodified guanosine. The tRNAs from both tissues also show significant quantitative differences in the chromatographic mobilities for isoaccepting species of tRNAAsp, tRNAAsn, tRNAHis and tRNATyr. In addition, chromatographic shifts upon cyanogen bromide treatment and analyses of the alkaline hydrolysates of these tRNAs demonstrate that those of tumour origin contain significantly less Q and Q nucleoside than their normal rat liver counterparts.

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Section: Resultsmentioning

confidence: 63%

“…A recent report by Olsen. and Penhoet [22] describing comparative studies of tRNATyr from human. placenta an.d HeLa cells indicates that no significant differences exist in.…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: C) Information Retrieval Limited 1 Falconberg Court London Wmentioning

confidence: 99%

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Comparison of rat liver and Walker 256 carcinosarcoma tRNAs

et al. 1979

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“…tRNAtYr and tRNAty3r, which were not well resolved by the chromatography conditions we employed, decreased gradually during the course of differentiation relative to the other species. Comparative studies of tRNAtyr from normal human placenta and HeLa cells indicated that no significant differences existed in the rate or site of incorporation of tyrosine into tryptic peptides of a-globin, even though there was again a dramatic difference in the RPC-5 chromatographic profiles between the tRNAs of these two tissues (17).…”

Section: Tymentioning

confidence: 94%

Specific changes in Q-ribonucleoside containing transfer RNA species during Friend leukemia cell erythroid differentiation

1980

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Changes in specific tRNA isoacceptors during Friend leukemia cell (F.L.C.) erythroid differentiation have been found to be concomitant with differences in the extent of the Q-base modification in certain species of tRNA. Transfer RNA was isolated from F.L.C. cultures after 0, 36, 48, 72, and 96 hr of DMSO induced differentiation. Changes in 17 isoacceptors of tRNAasn, tRNAasp, tRNAhis and tRNAtyr were compared by RPC-5 chromatography. Isoacceptors of these tRNA changed in relative amounts, following consistent trends throughout cell differentiation. The amount and distribution of Q-base containing tRNA isoacceptors was assayed by measuring the quanine-tRNA transferase catalyzed incorporation of [3H]-labeled guanine into tRNA species undermodified in Q-base followed by RPC-5 chormatography of the tRNA. The amount of Q-base containing tRNA species decreased in the first 48 hr after the induction, then increased again, indicating the level of Q-modification is correlated to the process of differentiation. Isoacceptors that lacked the Q-base were eluted late from RPC-5.

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Queuosine modification of the wobble base in tRNAHis influences ‘in vivo’ decoding properties.

Meier¹,

Suter²,

Grosjean³

et al. 1985

The EMBO Journal

150

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The 'in vivo' decoding properties of four tRNAHis isoacceptors, two from Drosophila melanogaster and two from brewer's yeast, were studied after their microinjection, along with turnip yellow mosaic virus (L'YMV) coat protein mRNA, into Xenopus laevis oocytes. The two Drosophila isoacceptors are identical besides containing either a guanosine (G) or the hypermodified nucleoside queuosine (Q) in the wobble position. The brewer's yeast isoacceptors differ by four bases in the anticodon stem, and by one base in the amino acceptor stem. Our results show that, under competing 'in vivo' conditions, the Drosophila tRNAHis with the anticodon GUG clearly prefers the histidine codon CAC to the codon CAU, whereas little preference is observed for the tRNAHis with the anticodon QUG for the codon CAU, and no preference for either codon by the two yeast isoacceptors. Hence, it can be concluded that the presence of the Q-base clearly affects the choice of the codon. This is the first demonstration of an 'in vivo' codon preference by tRNA isoacceptors differing in the modification of the wobble base during the elongation step of protein synthesis. These results imply that one function of the Q-base is at the translational level. Key words: decoding/modification/queuosine/transfer RNA/ wobble base as a sensitive assay system. The two Drosophila tRNAHis differ only by the presence or absence of the Q-base in the wobble position (Altwegg and and unpublished results), whereas the two brewer's yeast tRNAs differ by four bases in the anticodon stem and one base in the amino acid acceptor stem. They do not contain the Q-modification in the wobble position, i.e., they possess identical anticodons (Keith et al., 1983).Turnip yellow mosaic virus (TYMV) coat protein RNA contains three histidine codons (Figure 1): two CAU in the 5' and one CAC in the 3' half of the mRNA (Guilley and Briand, 1978). Cyanogen bromide cleavage of the coat protein at the methionine residues yields three peptides: one large fragment (X) of 135 amino acid residues, containing the two CAU coded histidines, one fragment of 42 amino acids containing no histidine, and a small fragment (Y) of 10 amino acid residues, containing the unique CAC coded histidine. Thus, it is possible to study the incorporation of histidine from each of the two tRNAH1s isoacceptors into the coat protein sites coded by the two histidine codons under competing conditions. TYMV coat protein mRNA, histidinol (inhibits the endogenous synthetase, Hansen et al., 1972), and equal amounts (pmol) of aminoacylated tRNA isoacceptors were injected into Xenopus oocytes and, after 4 h of incubation, the incorporation into the peptides X and Y determined.Since only [3H]histidine labelling provides the necessary specific activity needed for these experiments, only one of the isoacceptors could be labeled. The competing isoacceptor carried an unlabeled histidine. In order to exclude potential artefacts (e.g., heterogeneity of the oocytes) we calculated the percentages and ratios of histidine incorporation f...

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Chromatographic and functional comparison of human placenta and HeLa cell tyrosine transfer ribonucleic acids

Cited by 11 publications

References 19 publications

Comparison of rat liver and Walker 256 carcinosarcoma tRNAs

Comparison of rat liver and Walker 256 carcinosarcoma tRNAs

Specific changes in Q-ribonucleoside containing transfer RNA species during Friend leukemia cell erythroid differentiation

Queuosine modification of the wobble base in tRNAHis influences ‘in vivo’ decoding properties.

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