19F NMR studies of the solution structure and dynamics of 5-fluorouracil-substituted valine tRNA from Escherichia coli

Hardin, Charles C.

doi:10.31274/rtd-180813-13087

Cited by 3 publications

(29 citation statements)

References 115 publications

(237 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3A and 3B) shows that while there are similarities, each tRNA yields a unique characteristic spectrum. One notable similarity between the spectra is that in each case the peaks can be grouped into three categories based on (Horowitz et al, 1977;Hardin, 1984;Hardin et al, 1986) supporting the hypothesis that these groupings correspond to FUra residues in three distinct structural environments in the tRNA molecule: hydrogen-bonded bases in helical domains (upfield), non-hydrogen-bonded bases in loops (central), and FUra residues participa ting in tertiary interactions (downfield).…”

Section: Interaction With Proteinsmentioning

confidence: 69%

“…FUra-containing tRNA^®^ and tRNAj®^ can be separated into two isoaccepting species termed the A and B forms (Hills et al, 1983;Hardin, 1984). ^®F NMR spectra of the two forms differ by the shift of one ^^F peak from ca.…”

Section: Interaction With Proteinsmentioning

confidence: 99%

“…with the modified FUra in the A form being located at the site of the only dihydrouracil in the molecule (position 17), but conclusive evidence was not available (Hardin, 1984).…”

Section: Interaction With Proteinsmentioning

confidence: 99%

“…Several other preliminary peak assignments in the ^^F NMR spectrum of (FUra)tRNAj®^ have been made (Hardin, 1984). However, most of the reso nances remain unassigned, and need to be assigned to allow interpretation of spectral changes at the molecular level.…”

Section: Interaction With Proteinsmentioning

confidence: 99%

“…The purified tRNA accepted over 1400 pmol l^C-L-valine per A260 unit. FUra-substituted tRNAj®^ was resolved into two isoaccepting forms, (A) and (B), on an RPC-5 reverse phase chromatography column (Pearson et al, 1971), as described by Hardin (1984). Unless the two forms were required separately, a mixture contain ing mostly form B, obtained after BD-cellulose chromatography, was used in these studies.…”

Section: Purification Of Fura-substituted Trnaf^tmentioning

confidence: 99%

See 4 more Smart Citations

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

Gollnick

View full text Add to dashboard Cite

This reproduction was made from a copy of a manuscript sent to us for publication and microfilming. While the most advanced technology has been used to pho tograph and reproduce this manuscript, the quality of the reproduction is heavily dependent upon the quality of the material submitted. Pages in any manuscript may have indistinct print. In all cases the best available copy has been filmed.The following explanation of techniques is provided to help clarify notations which may appear on this reproduction.1. Manuscripts may not always be complete. When it is not possible to obtain missing pages, a note appears to indicate this.2. When copyrighted materials are removed from the manuscript, a note ap pears to indicate this. Oversize materials (maps, drawings, and charts) are photographed by sec tioning the original, beginning at the upper left hand comer and continuing from left to right in equal sections with small overlaps. Each oversize page is also filmed as one exposure and is available, for an additional charge, as a standard 35mm slide or in black and white paper format.* 4. Most photographs reproduce acceptably on positive microfilm or micro fiche but lack clarity on xerographic copies made from the microfilm. For an additional charge, all photographs are available in black and white standard 35mm slide format.*

show abstract

Section: Interaction With Proteinsmentioning

confidence: 69%

Section: Interaction With Proteinsmentioning

confidence: 99%

“…with the modified FUra in the A form being located at the site of the only dihydrouracil in the molecule (position 17), but conclusive evidence was not available (Hardin, 1984).…”

Section: Interaction With Proteinsmentioning

confidence: 99%

Section: Interaction With Proteinsmentioning

confidence: 99%

Section: Purification Of Fura-substituted Trnaf^tmentioning

confidence: 99%

See 3 more Smart Citations

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

Gollnick

View full text Add to dashboard Cite

show abstract

Combined in silico and 19F NMR analysis of 5-fluorouracil metabolism in yeast at low ATP conditions

et al. 2019

View full text Add to dashboard Cite

The cytotoxic effect of 5-fluorouracil (5-FU) on yeast cells is thought to be mainly via a misincorporation of fluoropyrimidines into both RNA and DNA, not only DNA damage via inhibition of thymidylate synthase (TYMS) by fluorodeoxyuridine monophosphate (FdUMP). However, some studies on Saccharomyces cerevisiae show a drastic decrease in ATP concentration under oxidative stress, together with a decrease in concentration of other tri- and diphosphates. This raises a question if hydrolysis of 5-fluoro-2-deoxyuridine diphosphate (FdUDP) under oxidative stress could not lead to the presence of FdUMP and the activation of so-called ‘thymine-less death’ route. We attempted to answer this question with in silico modeling of 5-FU metabolic pathways, based on new experimental results, where the stages of intracellular metabolism of 5-FU in Saccharomyces cerevisiae were tracked by a combination of 19F and 31P NMR spectroscopic study. We have identified 5-FU, its nucleosides and nucleotides, and subsequent di- and/or triphosphates. Additionally, another wide 19F signal, assigned to fluorinated unstructured short RNA, has been also identified in the spectra. The concentration of individual metabolites was found to vary substantially within hours, however, the initial steady-state was preserved only for an hour, until the ATP concentration dropped by a half, which was monitored independently via 31P NMR spectra. After that, the catabolic process leading from triphosphates through monophosphates and nucleosides back to 5-FU was observed. These results imply careful design and interpretation of studies in 5-FU metabolism in yeast.

show abstract

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

Gollnick

View full text Add to dashboard Cite

This reproduction was made from a copy of a manuscript sent to us for publication and microfilming. While the most advanced technology has been used to pho tograph and reproduce this manuscript, the quality of the reproduction is heavily dependent upon the quality of the material submitted. Pages in any manuscript may have indistinct print. In all cases the best available copy has been filmed.The following explanation of techniques is provided to help clarify notations which may appear on this reproduction. Manuscripts may not always be complete. When it is not possible to obtainmissing pages, a note appears to indicate this.2. When copyrighted materials are removed from the manuscript, a note ap pears to indicate this. Oversize materials (maps, drawings, and charts) are photographed by sec tioning the original, beginning at the upper left hand comer and continu ing from left to right in equal sections with small overlaps. Each oversize page is also filmed as one exposure and is available, for an additional charge, as a standard 35mm slide or in black and white paper format.* 4. Most photographs reproduce acceptably on positive microfilm or micro fiche but lack clarity on xerographic copies made from the microfilm. For an additional charge, all photographs are available in black and white standard 35mm slide format.*

show abstract

19F NMR studies of the solution structure and dynamics of 5-fluorouracil-substituted valine tRNA from Escherichia coli

Cited by 3 publications

References 115 publications

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

Combined in silico and 19F NMR analysis of 5-fluorouracil metabolism in yeast at low ATP conditions

19F NMR studies of 5-fluorouracil-substituted Escherichia coli transfer RNAs: solution structure and codon-anticodon interaction

Contact Info

Product

Resources

About