Publications
1996
de Barros J. P. Pais, Keith G., Adlouni C. El, Glasser A. L., Mack G., Dirheimer G., Desgres J.
2'-O-methyl-5-formylcytidine (f5Cm), a new modified nucleotide at the 'wobble' of two cytoplasmic tRNAs Leu (NAA) from bovine liver Journal Article
In: Nucleic Acids Res, vol. 24, no. 8, pp. 1489-96, 1996, (0305-1048 Journal Article).
Abstract | BibTeX | Tags: &, Acid, Acyl/*chemistry/isolation, Amino, Animals, Base, Borohydrides/chemistry, Cattle, Cells, Conformation, Cytidine/*analogs, Cytoplasm, Data, derivatives/chemistry/isolation, Fragmentography, Gov't, Hela, Human, Liver/*chemistry, Mass, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, structure, Support, Transfer
@article{,
title = {2'-O-methyl-5-formylcytidine (f5Cm), a new modified nucleotide at the 'wobble' of two cytoplasmic tRNAs Leu (NAA) from bovine liver},
author = { J. P. Pais de Barros and G. Keith and C. El Adlouni and A. L. Glasser and G. Mack and G. Dirheimer and J. Desgres},
year = {1996},
date = {1996-01-01},
journal = {Nucleic Acids Res},
volume = {24},
number = {8},
pages = {1489-96},
abstract = {The nucleotide analysis of a cytoplasmic tRNA(Leu) isolated from bovine liver revealed the presence of an unknown modified nucleotide N. The corresponding N nucleoside was isolated by different enzymatic and chromatographic protocols from a partially purified preparation of this tRNA(Leu). Its chemical characterization was determined from its chromatographic properties, UV-absorption spectroscopy and mass spectrometric measurements, as well as from those of the borohydride reduced N nucleoside and its etheno-trimethylsilyl derivative. The structure of N was established as 2'-O-methyl-5-formylcytidine (f5CM), and its reduced derivative as 2'-O-methyl-5-hydroxy-methylcytidine (om5Cm). By sequencing the bovine liver tRNA(Leu), the structure of the anticodon was determined as f5CmAA. In addition, the nucleotide sequence showed two primary structures differing only by the nucleotide 47c which is either uridine or adenosine. The two slightly differing bovine liver tRNAs-Leu(f5CmAA) are the only tRNAs so far sequenced which contain f5Cm. The role of such a modified cytidine at the first position of the anticodon is discussed in terms of decoding properties for the UUG and UUA leucine codons. Recently, precise evidence was obtained for the presence of f5Cm at the same position in tRNAs(Leu)(NAA) isolated from rabbit and lamb liver. Therefore, the 2'-O-methyl-5-formyl modification of cytidine at position 34 could be a general feature of cytoplasmic tRNAs(Leu)(NAA) in mammals.},
note = {0305-1048
Journal Article},
keywords = {&, Acid, Acyl/*chemistry/isolation, Amino, Animals, Base, Borohydrides/chemistry, Cattle, Cells, Conformation, Cytidine/*analogs, Cytoplasm, Data, derivatives/chemistry/isolation, Fragmentography, Gov't, Hela, Human, Liver/*chemistry, Mass, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, structure, Support, Transfer},
pubstate = {published},
tppubtype = {article}
}
1992
Nothwang H. G., Coux O., Keith G., Silva-Pereira I., Scherrer K.
The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3) Journal Article
In: Nucleic Acids Res, vol. 20, no. 8, pp. 1959-65, 1992, (0305-1048 Journal Article).
Abstract | BibTeX | Tags: Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology
@article{,
title = {The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3)},
author = { H. G. Nothwang and O. Coux and G. Keith and I. Silva-Pereira and K. Scherrer},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {8},
pages = {1959-65},
abstract = {Two-dimensional gel electrophoresis of HeLa cell prosomal RNAs, 3'-end labeled by RNA ligase, revealed one prominent spot. Determination of a partial sequence at the 3'-end indicated full homology to the 18 nucleotides at the 3'-end of tRNA(Lys,3) from rabbit, the bovine and the human species. An oligonucleotide complementary to the 3'-end of tRNA(Lys,3) hybridized on Northern blots with prosomal RNA from both HeLa cells and duck erythroblasts. In two-dimensional PAGE, the major pRNA of HeLa cells co-migrated with bovine tRNA(Lys,3). Reconstitution of the CCA 3'-end of RNA from both human and duck prosomes, by tRNA-nucleotidyl-transferase, confirmed the tRNA character of this type of RNA. Furthermore, it revealed at least one additional tRNA band about 85 nt long among the prosomal RNA from both species. Finally, confirming an original property of prosomal RNA, we show that in vitro synthesized tRNA(Lys,3) hybridizes stably to duck globin mRNA, and to poly(A)(+)- and poly(A)(-)-RNA from HeLa cells.},
note = {0305-1048
Journal Article},
keywords = {Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology},
pubstate = {published},
tppubtype = {article}
}