Heyman T., Agoutin B., Fix C., Dirheimer G., Keith G.
Yeast serine isoacceptor tRNAs: variations of their content as a function of growth conditions and primary structure of the minor tRNA(Ser)GCU Article de journal
Dans: FEBS Lett, vol. 347, no. 2-3, p. 143-6, 1994, (0014-5793 Journal Article).
Résumé | BibTeX | Étiquettes: &, Acid, Anticodon, Base, cerevisiae/*genetics/*growth, Conformation, Culture, Data, development, Fungal/*chemistry, Galactose, Hybridization, Media, Molecular, Nucleic, Probes, RNA, Saccharomyces, Sequence, Ser/analysis/*chemistry, Transfer, Transfer/*chemistry
@article{,
title = {Yeast serine isoacceptor tRNAs: variations of their content as a function of growth conditions and primary structure of the minor tRNA(Ser)GCU},
author = { T. Heyman and B. Agoutin and C. Fix and G. Dirheimer and G. Keith},
year = {1994},
date = {1994-01-01},
journal = {FEBS Lett},
volume = {347},
number = {2-3},
pages = {143-6},
abstract = {The primary structure of Saccharomyces cerevisiae tRNA(Ser)GCU is presented (EMBL database accession No. X74268 S. cerevisiae tRNA-Ser). In addition, quantitation of the relative amounts of serine isoaccepting tRNAs in yeast grown on different media showed that the minor tRNA(Ser)GCU decreased while the major tRNA(Ser)AGA increased as the growth rate and the cellular protein content increased. The minor species, tRNA(Ser)CGA and tRNA(Ser)UGA, were not separated by our gel system, however, taken together they appeared to vary in the same way as tRNA(Ser)GCU. These data suggest a growth rate dependence of yeast tRNAs similar to that previously described for E. coli tRNAs.},
note = {0014-5793
Journal Article},
keywords = {&, Acid, Anticodon, Base, cerevisiae/*genetics/*growth, Conformation, Culture, Data, development, Fungal/*chemistry, Galactose, Hybridization, Media, Molecular, Nucleic, Probes, RNA, Saccharomyces, Sequence, Ser/analysis/*chemistry, Transfer, Transfer/*chemistry},
pubstate = {published},
tppubtype = {article}
}
el Adlouni C., Keith G., Dirheimer G., Szarkowski J. W., Przykorska A.
Rye nuclease I as a tool for structural studies of tRNAs with large variable arms Article de journal
Dans: Nucleic Acids Res, vol. 21, no. 4, p. 941-7, 1993, (0305-1048 Journal Article).
Résumé | BibTeX | Étiquettes: *Nucleotidases, Acid, Animals, Anticodon, Base, Cattle, cereale/*enzymology, cerevisiae, Conformation, Data, Gov't, Leu/chemistry, Molecular, Non-U.S., Nucleic, RNA, Saccharomyces, Secale, Sequence, Ser/chemistry, Support, Transfer, Transfer/*chemistry
@article{,
title = {Rye nuclease I as a tool for structural studies of tRNAs with large variable arms},
author = { C. el Adlouni and G. Keith and G. Dirheimer and J. W. Szarkowski and A. Przykorska},
year = {1993},
date = {1993-01-01},
journal = {Nucleic Acids Res},
volume = {21},
number = {4},
pages = {941-7},
abstract = {A single-strand-specific nuclease from rye germ (Rn nuclease I) was used for secondary and tertiary structure investigations of tRNAs with large variable arms (class II tRNAs). We have studied the structure in solution of two recently sequenced tRNA(Leu): yeast tRNA(Leu)(ncm5UmAA) and bovine tRNA(Leu)(XmAA) as well as yeast tRNA(Leu)(UAG), tRNA(Leu)(m5CAA) and tRNA(Ser)(IGA). The latter is the only tRNA with a long variable arm for which the secondary and tertiary structure has already been studied by use of chemical probes and computer modelling. The data obtained in this work showed that the general model of class II tRNAs proposed by others for tRNA(Ser) can be extended to tRNAs(Leu) as well. However interesting differences in the structure of tRNAs(Leu) versus tRNA(Ser)(IGA) were also noticed. The main difference was observed in the accessibility of the variable loops to nucleolytic attack of Rn nuclease I: variable loops of all studied tRNA(Leu) species were cut by Rn nuclease I, while that of yeast tRNA(Ser)(IGA) was not. This could be due to differences in stability of the variable arms and the lengths of their loops which are 3 and 4 nucleotides in tRNA(Ser)(IGA) and tRNAs(Leu) respectively.},
note = {0305-1048
Journal Article},
keywords = {*Nucleotidases, Acid, Animals, Anticodon, Base, Cattle, cereale/*enzymology, cerevisiae, Conformation, Data, Gov't, Leu/chemistry, Molecular, Non-U.S., Nucleic, RNA, Saccharomyces, Secale, Sequence, Ser/chemistry, Support, Transfer, Transfer/*chemistry},
pubstate = {published},
tppubtype = {article}
}