The role of queuine in the aminoacylation of mammalian aspartate transfer RNAs

Singhal, Ram P.; Vakharia, Vikram N.

doi:10.1093/nar/11.12.4257

Cited by 20 publications

(10 citation statements)

References 29 publications

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“…Characteristically the seven membered loop of stem 11 contains the sequence UUCG and is connected to a G-C base pair of the stem. This sequence, reminiscent of the TkCG sequence of tRNA (Singhal and Fallis, 1979), was noted earlier in the tRNA-like structures of BMV, BBMV, CCMV and CMV RNA in the corresponding position (compare Figure 5E). For TMV RNA it was shown that the ribothymidineforming tRNA methyltransferase from Escherichia coli could quantitatively methylate the first U from the UUCG sequence in stem 11 (Lesiewicz and Dudock, 1978), as is the case in normal tRNAs.…”

Section: Discussionsupporting

confidence: 63%

The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice

et al. 1984

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The structure of the tRNA‐like 3′ terminus of tobacco mosaic virus (TMV) RNA has been studied. A 3′ ‐terminal fragment possessing the tRNA‐like properties was probed with chemical modification and enzymatic digestions. A model of the secondary structure is proposed for the last 105 nucleotides. The corresponding region of other tobamoviral RNAs can be folded in an identical secondary structure. A three‐dimensional model for the tRNA‐like structure is given which is compared with those proposed earlier for the tRNA‐like 3′ termini of turnip yellow mosaic virus (TYMV) RNA and brome mosaic virus (BMV) RNA. A new building principle which we discovered previously by studying the latter RNAs appears to be applied twice in the tRNA‐like structure of TMV RNA. The determination of the minimal length requirement for recognition of CTP, ATP:tRNA nucleotidyl‐transferase reveals a size of ˜100 nucleotides in agreement with the models proposed.

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Section: Discussionsupporting

confidence: 63%

The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice

et al. 1984

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“…The data presented strongly support the conclusion that the functional mt-tRNAs of nematode worms are direct transcripts (with only CCA addition) of the structurally unusual mt-tRNA genes. There is no evidence of trans-splicing or RNA Introduction Throughout the evolution of prokaryotes, animals and plants, the primary and secondary structures of transfer RNAs (tRNAs), and the genes that encode them, have been highly conserved (Dirheimer et al, 1979;Singhal and Fallis, 1979;Sprinzl et al, 1989). Only among the mitochondrial DNAs (mtDNAs) of metazoa are major tRNA gene sequence deviations found.…”

mentioning

confidence: 99%

A set of tRNAs that lack either the T psi C arm or the dihydrouridine arm: towards a minimal tRNA adaptor.

1990

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The mitochondrial DNA (mtDNA) molecules of the nematode worms, Caenorhabditis elegans and Ascaris suum contain 22 putative genes for non‐standard forms of tRNAs. The inferred transcripts can be folded into 20 separate structures each resembling a tRNA whose T psi C arm and variable loop are replaced with a simple loop of 6‐12 nucleotides. In two further structures [that resemble tRNAs for ser(UCN) and ser(AGN)], the dihydrouridine arm is replaced by a loop of 5‐8 nucleotides. By hybridizing mt‐tRNA gene‐specific oligonucleotide probes to nematode RNAs, we have obtained evidence for transcription of at least nine C.elegans and three A.suum mt‐tRNA genes. Each transcript (tRNA) is the exact size predicted from the respective DNA sequence, to which three nucleotides, presumably CCA, have been added following transcription. An exception was C.elegans mt‐tRNAasn, most molecules of which had one nucleotide (plus CCA) more than predicted from the gene. The data presented strongly support the conclusion that the functional mt‐tRNAs of nematode worms are direct transcripts (with only CCA addition) of the structurally unusual mt‐tRNA genes. There is no evidence of trans‐splicing or RNA editing to add the sequences missing from these nonstandard tRNAs. We presume, therefore, that the non‐standard forms are active in mitochondrial protein synthesis.

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“…It should be noted that the Q-hypomodification is not a universal phenomenon of cancer. Some studies have shown fully Q-modified tRNA in patient neoplastic samples [ 59 , 131 , 132 ]. Nevertheless, where hypomodification does occur, it appears to correlate strongly with the tumor grade [ 59 , 128 , 129 , 130 , 131 ].…”

Section: Queuine and Queuosine In Cancermentioning

confidence: 99%

“…Studies indicate that the presence of queuosine can affect the efficiency of tRNA aminoacylation. Using rabbit liver aminoacyl tRNA synthetase and unfractionated tRNA preparations from L-M cells it was found that Q-modified aspartyl tRNA had a 30% higher V max and 55% lower K m for amino acid charging relative to G-containing aspartyl tRNA [ 132 ]. Similarly, the presence of Q 34 in tyrosyl tRNA from E.coli results in a slight decrease in K m (0.47 µM) relative to G 34 (0.6 µM) [ 35 ].…”

Section: Queuosine In Translationmentioning

confidence: 99%

The Queuine Micronutrient: Charting a Course from Microbe to Man

et al. 2015

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Micronutrients from the diet and gut microbiota are essential to human health and wellbeing. Arguably, among the most intriguing and enigmatic of these micronutrients is queuine, an elaborate 7-deazaguanine derivative made exclusively by eubacteria and salvaged by animal, plant and fungal species. In eubacteria and eukaryotes, queuine is found as the sugar nucleotide queuosine within the anticodon loop of transfer RNA isoacceptors for the amino acids tyrosine, asparagine, aspartic acid and histidine. The physiological requirement for the ancient queuine molecule and queuosine modified transfer RNA has been the subject of varied scientific interrogations for over four decades, establishing relationships to development, proliferation, metabolism, cancer, and tyrosine biosynthesis in eukaryotes and to invasion and proliferation in pathogenic bacteria, in addition to ribosomal frameshifting in viruses. These varied effects may be rationalized by an important, if ill-defined, contribution to protein translation or may manifest from other presently unidentified mechanisms. This article will examine the current understanding of queuine uptake, tRNA incorporation and salvage by eukaryotic organisms and consider some of the physiological consequence arising from deficiency in this elusive and lesser-recognized micronutrient.

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The role of queuine in the aminoacylation of mammalian aspartate transfer RNAs

Cited by 20 publications

References 29 publications

The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice

The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice

A set of tRNAs that lack either the T psi C arm or the dihydrouridine arm: towards a minimal tRNA adaptor.

The Queuine Micronutrient: Charting a Course from Microbe to Man

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