Publications
2004
Zhang H, Kolb F A, Jaskiewicz L, Westhof E, Filipowicz W
Single processing center models for human Dicer and bacterial RNase III Journal Article
In: Cell, vol. 118, no. 1, pp. 57-68, 2004, ISBN: 15242644, (0092-8674 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Base Sequence Comparative Study Conserved Sequence Dimerization Endoribonucleases/*chemistry/genetics/isolation & purification/*metabolism Escherichia coli/enzymology Human Manganese/metabolism MicroRNAs/metabolism Models, Double-Stranded/chemistry/*metabolism RNA, Molecular Molecular Sequence Data Molecular Weight Mutagenesis, Non-U.S. Gov't, Post-Transcriptional RNA, Secondary Protein Structure, Site-Directed Mutation Protein Structure, Small Interfering/metabolism Recombinant Proteins/metabolism Ribonuclease III/*chemistry/genetics/isolation & purification/*metabolism Sequence Homology, Tertiary RNA Helicases/*chemistry/genetics/isolation & purification/*metabolism *RNA Processing, Unité ARN, WESTHOF
@article{,
title = {Single processing center models for human Dicer and bacterial RNase III},
author = {H Zhang and F A Kolb and L Jaskiewicz and E Westhof and W Filipowicz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15242644},
isbn = {15242644},
year = {2004},
date = {2004-01-01},
journal = {Cell},
volume = {118},
number = {1},
pages = {57-68},
abstract = {Dicer is a multidomain ribonuclease that processes double-stranded RNAs (dsRNAs) to 21 nt small interfering RNAs (siRNAs) during RNA interference, and excises microRNAs from precursor hairpins. Dicer contains two domains related to the bacterial dsRNA-specific endonuclease, RNase III, which is known to function as a homodimer. Based on an X-ray structure of the Aquifex aeolicus RNase III, models of the enzyme interaction with dsRNA, and its cleavage at two composite catalytic centers, have been proposed. We have generated mutations in human Dicer and Escherichia coli RNase III residues implicated in the catalysis, and studied their effect on RNA processing. Our results indicate that both enzymes have only one processing center, containing two RNA cleavage sites and generating products with 2 nt 3' overhangs. Based on these and other data, we propose that Dicer functions through intramolecular dimerization of its two RNase III domains, assisted by the flanking RNA binding domains, PAZ and dsRBD.},
note = {0092-8674
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Base Sequence Comparative Study Conserved Sequence Dimerization Endoribonucleases/*chemistry/genetics/isolation & purification/*metabolism Escherichia coli/enzymology Human Manganese/metabolism MicroRNAs/metabolism Models, Double-Stranded/chemistry/*metabolism RNA, Molecular Molecular Sequence Data Molecular Weight Mutagenesis, Non-U.S. Gov't, Post-Transcriptional RNA, Secondary Protein Structure, Site-Directed Mutation Protein Structure, Small Interfering/metabolism Recombinant Proteins/metabolism Ribonuclease III/*chemistry/genetics/isolation & purification/*metabolism Sequence Homology, Tertiary RNA Helicases/*chemistry/genetics/isolation & purification/*metabolism *RNA Processing, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
2003
Rigourd M, Goldschmidt V, Brule F, Morrow C D, Ehresmann B, Ehresmann C, Marquet R
Structure-function relationships of the initiation complex of HIV-1 reverse transcription: the case of mutant viruses using tRNA(His) as primer Journal Article
In: Nucleic Acids Res, vol. 31, no. 19, pp. 5764-5775, 2003, ISBN: 14500840, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence Comparative Study DNA, Genetic, Genetic *Transcription Initiation Site *Transcription, His/*metabolism RNA, MARQUET, Non-U.S. Gov't Templates, Post-Transcriptional RNA, Transfer, Unité ARN, Viral HIV-1/*genetics/metabolism HIV-1 Reverse Transcriptase/metabolism Kinetics Macromolecular Systems Molecular Sequence Data Mutation RNA Probes RNA Processing, Viral/*biosynthesis/genetics Sequence Alignment Structure-Activity Relationship Support, Viral/biosynthesis *Gene Expression Regulation
@article{,
title = {Structure-function relationships of the initiation complex of HIV-1 reverse transcription: the case of mutant viruses using tRNA(His) as primer},
author = {M Rigourd and V Goldschmidt and F Brule and C D Morrow and B Ehresmann and C Ehresmann and R Marquet},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14500840},
isbn = {14500840},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {19},
pages = {5764-5775},
abstract = {Reverse transcription of HIV-1 RNA is initiated from the 3' end of a tRNA3Lys molecule annealed to the primer binding site (PBS). An additional interaction between the anticodon loop of tRNA3Lys and a viral A-rich loop is required for efficient initiation of reverse transcription of the HIV-1 MAL isolate. In the HIV-1 HXB2 isolate, simultaneous mutations of the PBS and the A-rich loop (mutant His-AC), but not of the PBS alone (mutant His) allows the virus to stably utilize tRNA(His) as primer. However, mutant His-AC selects additional mutations during cell culture, generating successively His-AC-GAC and His-AC-AT-GAC. Here, we wanted to establish direct relationships between the evolution of these mutants in cell culture, their efficiency in initiating reverse transcription and the structure of the primer/template complexes in vitro. The initiation of reverse transcription of His and His-AC RNAs was dramatically reduced. However, His-AC-GAC RNA, which incorporated three adaptative point mutations, was reverse transcribed more efficiently than the wild type RNA. Incorporation of two additional mutations decreased the efficiency of the initiation of reverse transcription, which remained at the wild type level. Structural probing showed that even though both His-AC and His-AC-GAC RNAs can potentially interact with the anticodon loop of tRNA(His), only the latter template formed a stable interaction. Thus, our results showed that the selection of adaptative mutations by HIV-1 mutants utilizing tRNA(His) as primer was initially dictated by the efficiency of the initiation of reverse transcription, which relied on the existence of a stable interaction between the mutated A-rich loop and the anticodon loop of tRNA(His).},
note = {1362-4962
Journal Article},
keywords = {Base Sequence Comparative Study DNA, Genetic, Genetic *Transcription Initiation Site *Transcription, His/*metabolism RNA, MARQUET, Non-U.S. Gov't Templates, Post-Transcriptional RNA, Transfer, Unité ARN, Viral HIV-1/*genetics/metabolism HIV-1 Reverse Transcriptase/metabolism Kinetics Macromolecular Systems Molecular Sequence Data Mutation RNA Probes RNA Processing, Viral/*biosynthesis/genetics Sequence Alignment Structure-Activity Relationship Support, Viral/biosynthesis *Gene Expression Regulation},
pubstate = {published},
tppubtype = {article}
}
Levinger L, Giege R, Florentz C
Pathology-related substitutions in human mitochondrial tRNA(Ile) reduce precursor 3' end processing efficiency in vitro Journal Article
In: Nucleic Acids Res, vol. 31, no. 7, pp. 1904-1912, 2003, ISBN: 12655007, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence DNA, FLORENTZ, Ile/*genetics/metabolism Support, Mitochondrial/*genetics Endoribonucleases/metabolism Hela Cells Human Kinetics Molecular Sequence Data Mutation RNA Precursors/genetics/metabolism *RNA Processing, Non-U.S. Gov't Support, P.H.S., Post-Transcriptional RNA, Transfer, U.S. Gov't, Unité ARN
@article{,
title = {Pathology-related substitutions in human mitochondrial tRNA(Ile) reduce precursor 3' end processing efficiency in vitro},
author = {L Levinger and R Giege and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12655007},
isbn = {12655007},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {7},
pages = {1904-1912},
abstract = {The human mitochondrial genome encodes 22 tRNAs interspersed among the two rRNAs and 11 mRNAs, often without spacers, suggesting that tRNAs must be efficiently excised. Numerous maternally transmitted diseases and syndromes arise from mutations in mitochondrial tRNAs, likely due to defect(s) in tRNA metabolism. We have systematically explored the effect of pathogenic mutations on tRNA(Ile) precursor 3' end maturation in vitro by 3'-tRNase. Strikingly, four pathogenic tRNA(Ile) mutations reduce 3'-tRNase processing efficiency (V(max) / K(M)) to approximately 10-fold below that of wild-type, principally due to lower V(max). The structural impact of mutations was sought by secondary structure probing and wild-type tRNA(Ile) precursor was found to fold into a canonical cloverleaf. Among the mutant tRNA(Ile) precursors with the greatest 3' end processing deficiencies, only G4309A displays a secondary structure substantially different from wild-type, with changes in the T domain proximal to the substitution. Reduced efficiency of tRNA(Ile) precursor 3' end processing, in one case associated with structural perturbations, could thus contribute to human mitochondrial diseases caused by mutant tRNAs.},
note = {1362-4962
Journal Article},
keywords = {Base Sequence DNA, FLORENTZ, Ile/*genetics/metabolism Support, Mitochondrial/*genetics Endoribonucleases/metabolism Hela Cells Human Kinetics Molecular Sequence Data Mutation RNA Precursors/genetics/metabolism *RNA Processing, Non-U.S. Gov't Support, P.H.S., Post-Transcriptional RNA, Transfer, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2001
Senger B, Lafontaine D L, Graindorge J S, Gadal O, Camasses A, Sanni A, Garnier J M, Breitenbach M, Hurt E, Fasiolo F
The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis Journal Article
In: Mol Cell, vol. 8, no. 6, pp. 1363-1373, 2001, ISBN: 11779510, (1097-2765 Journal Article).
Abstract | Links | BibTeX | Tags: Biological Transport Cell Division Cell Nucleolus/*metabolism Cell Nucleus/*metabolism Conserved Sequence Cytoplasm/enzymology/*metabolism Enzyme Activation GTP Phosphohydrolases/chemistry/genetics/*metabolism Gene Deletion Genes, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't, Post-Transcriptional RNA, Reporter/genetics Molecular Weight Phenotype Protein Subunits RNA Precursors/chemistry/genetics/metabolism *RNA Processing, Ribosomal/chemistry/genetics/metabolism Ribosomes/chemistry/*metabolism Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism Support, Unité ARN
@article{,
title = {The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis},
author = {B Senger and D L Lafontaine and J S Graindorge and O Gadal and A Camasses and A Sanni and J M Garnier and M Breitenbach and E Hurt and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11779510},
isbn = {11779510},
year = {2001},
date = {2001-01-01},
journal = {Mol Cell},
volume = {8},
number = {6},
pages = {1363-1373},
abstract = {Deletion of elongation factor-like 1 (Efl1p), a cytoplasmic GTPase homologous to the ribosomal translocases EF-G/EF-2, results in nucle(ol)ar pre-rRNA processing and pre-60S subunits export defects. Efl1p interacts genetically with Tif6p, a nucle(ol)ar protein stably associated with pre-60S subunits and required for their synthesis and nuclear exit. In the absence of Efl1p, 50% of Tif6p is relocated to the cytoplasm. In vitro, the GTPase activity of Efl1p is stimulated by 60S, and Efl1p promotes the dissociation of Tif6p-60S complexes. We propose that Tif6p binds to the pre-60S subunits in the nucle(ol)us and escorts them to the cytoplasm where the GTPase activity of Efl1p triggers a late structural rearrangement, which facilitates the release of Tif6p and its recycling to the nucle(ol)us.},
note = {1097-2765
Journal Article},
keywords = {Biological Transport Cell Division Cell Nucleolus/*metabolism Cell Nucleus/*metabolism Conserved Sequence Cytoplasm/enzymology/*metabolism Enzyme Activation GTP Phosphohydrolases/chemistry/genetics/*metabolism Gene Deletion Genes, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't, Post-Transcriptional RNA, Reporter/genetics Molecular Weight Phenotype Protein Subunits RNA Precursors/chemistry/genetics/metabolism *RNA Processing, Ribosomal/chemistry/genetics/metabolism Ribosomes/chemistry/*metabolism Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Schiffer S, Helm M, Théobald-Dietrich A, Giege R, Marchfelder A
The plant tRNA 3' processing enzyme has a broad substrate spectrum Journal Article
In: Biochemistry, vol. 40, no. 28, pp. 8264-8272, 2001, ISBN: 11444972, (0006-2960 Journal Article).
Abstract | Links | BibTeX | Tags: Non-U.S. Gov't, Plant/genetics/*metabolism RNA, Post-Transcriptional RNA, Transfer, Tyr/genetics/*metabolism Substrate Specificity/genetics Support, Unité ARN
@article{,
title = {The plant tRNA 3' processing enzyme has a broad substrate spectrum},
author = {S Schiffer and M Helm and A Théobald-Dietrich and R Giege and A Marchfelder},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11444972},
isbn = {11444972},
year = {2001},
date = {2001-01-01},
journal = {Biochemistry},
volume = {40},
number = {28},
pages = {8264-8272},
abstract = {To elucidate the minimal substrate for the plant nuclear tRNA 3' processing enzyme, we synthesized a set of tRNA variants, which were subsequently incubated with the nuclear tRNA 3' processing enzyme. Our experiments show that the minimal substrate for the nuclear RNase Z consists of the acceptor stem and T arm. The broad substrate spectrum of the nuclear RNase Z raises the possibility that this enzyme might have additional functions in the nucleus besides tRNA 3' processing. Incubation of tRNA variants with the plant mitochondrial enzyme revealed that the organellar counterpart of the nuclear enzyme has a much narrower substrate spectrum. The mitochondrial RNase Z only tolerates deletion of anticodon and variable arms and only with a drastic reduction in cleavage efficiency, indicating that the mitochondrial activity can only cleave bona fide tRNA substrates efficiently. Both enzymes prefer precursors containing short 3' trailers over extended 3' additional sequences. Determination of cleavage sites showed that the cleavage site is not shifted in any of the tRNA variant precursors.},
note = {0006-2960
Journal Article},
keywords = {Non-U.S. Gov't, Plant/genetics/*metabolism RNA, Post-Transcriptional RNA, Transfer, Tyr/genetics/*metabolism Substrate Specificity/genetics Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2000
Fechter P, Rudinger-Thirion J, Théobald-Dietrich A, Giege R
Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features Journal Article
In: Biochemistry, vol. 39, no. 7, pp. 1725-1733, 2000, ISBN: 10677221, (0006-2960 Journal Article).
Abstract | Links | BibTeX | Tags: Acylation Anticodon/chemistry/metabolism Base Sequence Escherichia coli/enzymology/genetics Heat Methanococcus/enzymology/genetics Molecular Mimicry Molecular Sequence Data Nucleic Acid Denaturation RNA Processing, Fungal/chemistry/*metabolism RNA, Non-U.S. Gov't Tyrosine/chemistry/*metabolism Tyrosine-tRNA Ligase/chemistry/*metabolism, Post-Transcriptional RNA, Transfer, Tyr/chemistry/*metabolism Saccharomyces cerevisiae/*enzymology/genetics Structure-Activity Relationship Support, Unité ARN
@article{,
title = {Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features},
author = {P Fechter and J Rudinger-Thirion and A Théobald-Dietrich and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10677221},
isbn = {10677221},
year = {2000},
date = {2000-01-01},
journal = {Biochemistry},
volume = {39},
number = {7},
pages = {1725-1733},
abstract = {The specific aminoacylation of tRNA by yeast tyrosyl-tRNA synthetase does not rely on the presence of modified residues in tRNA(Tyr), although such residues stabilize its structure. Thus, the major tyrosine identity determinants were searched by the in vitro approach using unmodified transcripts produced by T7 RNA polymerase. On the basis of the tyrosylation efficiency of tRNA variants, the strongest determinants are base pair C1-G72 and discriminator residue A73 (the 5'-phosphoryl group on C1, however, is unimportant for tyrosylation). The three anticodon bases G34, U35, and A36 contribute also to the tyrosine identity, but to a lesser extent, with G34 having the most pronounced effect. Mutation of the GUA tyrosine anticodon into a CAU methionine anticodon, however, leads to a loss of tyrosylation efficiency similar to that obtained after mutation of the C1-G72 or A73 determinants. Transplantation of the six determinants into four different tRNA frameworks and activity assays on heterologous Escherichia coli and Methanococcus jannaschii tRNA(Tyr) confirmed the completeness of the tyrosine set and the eukaryotic character of the C1-G72 base pair. On the other hand, it was found that tyrosine identity in yeast does not rely on fine architectural features of the tRNA, in particular the size and sequence of the D-loop. Noticeable, yeast TyrRS efficiently charges a variant of E. coli tRNA(Tyr) with a large extra-region provided its G1-C72 base pair is changed to a C1-G72 base pair. Finally, tyrosylation activity is compatible with a +1 shift of the anticodon in the 3'-direction but is strongly inhibited if this shift occurs in the opposite 5'-direction.},
note = {0006-2960
Journal Article},
keywords = {Acylation Anticodon/chemistry/metabolism Base Sequence Escherichia coli/enzymology/genetics Heat Methanococcus/enzymology/genetics Molecular Mimicry Molecular Sequence Data Nucleic Acid Denaturation RNA Processing, Fungal/chemistry/*metabolism RNA, Non-U.S. Gov't Tyrosine/chemistry/*metabolism Tyrosine-tRNA Ligase/chemistry/*metabolism, Post-Transcriptional RNA, Transfer, Tyr/chemistry/*metabolism Saccharomyces cerevisiae/*enzymology/genetics Structure-Activity Relationship Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1997
Grosjean H, Szweykowska-Kulinska Z, Motorin Y, Fasiolo F, Simos G
Intron-dependent enzymatic formation of modified nucleosides in eukaryotic tRNAs: a review Journal Article
In: Biochimie, vol. 79, no. 5, pp. 293-302, 1997, ISBN: 9258438, (0300-9084 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Animals Base Sequence Eukaryotic Cells *Introns Molecular Sequence Data Nucleosides/*metabolism *RNA Processing, Non-U.S. Gov't tRNA Methyltransferases/*metabolism, Post-Transcriptional RNA, Transfer/genetics/*metabolism Support, Unité ARN
@article{,
title = {Intron-dependent enzymatic formation of modified nucleosides in eukaryotic tRNAs: a review},
author = {H Grosjean and Z Szweykowska-Kulinska and Y Motorin and F Fasiolo and G Simos},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9258438},
isbn = {9258438},
year = {1997},
date = {1997-01-01},
journal = {Biochimie},
volume = {79},
number = {5},
pages = {293-302},
abstract = {In eukaryotic cells, especially in yeast, several genes encoding tRNAs contain introns. These are removed from pre-tRNAs during the maturation process by a tRNA-specific splicing machinery that is located within the nucleus at the nuclear envelope. Before and after the intron removal, several nucleoside modifications are added in a stepwise manner, but most of them are introduced prior to intron removal. Some of these early nucleoside modifications are catalyzed by intron-dependent enzymes while most of the others are catalyzed in an intron-independent manner. In the present paper, we review all known cases where the nucleoside modifications were shown to depend strictly on the presence of an intron. These are pseudouridines at anticodon positions 34, 35 and 36 and 5-methylcytosine at position 34 of several eukaryotic tRNAs. One common property of the corresponding intron-dependent modifying enzymes is that their activities are essentially dependent on the local specific architecture of the pre-tRNA molecule that comprises the anticodon stem and loop prolonged by the intron domain. Thus introns clearly serve as internal (cis-type) RNAs that guide nucleoside modifications by providing transient target sites in tRNA for selected nuclear modifying enzymes. This situation may be similar to the recently discovered (trans-type) snoRNA-guided process of ribose methylations of ribosomal RNAs within the nucleolus of eukaryotic cells.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Animals Base Sequence Eukaryotic Cells *Introns Molecular Sequence Data Nucleosides/*metabolism *RNA Processing, Non-U.S. Gov't tRNA Methyltransferases/*metabolism, Post-Transcriptional RNA, Transfer/genetics/*metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1996
Yusupova G, Lanchy J M, Yusupov M, Keith G, Grice S F Le, Ehresmann C, Ehresmann B, Marquet R
Primer selection by HIV-1 reverse transcriptase on RNA-tRNA(3Lys) and DNA-tRNA(3Lys) hybrids Journal Article
In: J Mol Biol, vol. 261, no. 3, pp. 315-321, 1996, ISBN: 8780773, (0022-2836 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence DNA, Lys/genetics/*metabolism RNA, MARQUET, Non-U.S. Gov't Support, P.H.S., Post-Transcriptional RNA, Transfer, U.S. Gov't, Unité ARN, Viral/genetics HIV-1/*enzymology/genetics HIV-1 Reverse Transcriptase Human Molecular Sequence Data *RNA Processing, Viral/genetics RNA-Directed DNA Polymerase/genetics/*metabolism Support
@article{,
title = {Primer selection by HIV-1 reverse transcriptase on RNA-tRNA(3Lys) and DNA-tRNA(3Lys) hybrids},
author = {G Yusupova and J M Lanchy and M Yusupov and G Keith and S F Le Grice and C Ehresmann and B Ehresmann and R Marquet},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8780773},
isbn = {8780773},
year = {1996},
date = {1996-01-01},
journal = {J Mol Biol},
volume = {261},
number = {3},
pages = {315-321},
abstract = {During reverse transcription of the genomic RNA of human immunodeficiency virus type 1 (HIV-1) into double-stranded DNA, reverse transcriptase (RT) must accommodate RNA-RNA, DNA-RNA, RNA-DNA and DNA-DNA hybrids as primer-template. In this study, we examined extension of RNA-tRNA3Lys, and DNA-tRNA3Lys complexes by HIV-1 RT. When the 3' end of tRNA3Lys is annealed to oligoribonucleotides, tRNA3Lys, but not the complementary RNAs, is extended by HIV-1 RT, indicating that tRNA3Lys is efficiently used as primer and RNA as template. An opposite primer usage is observed when tRNA3Lys is annealed to complementary oligodeoxyribonucleotides. In this case, the oligodeoxyribonucleotides are efficiently used as primer and tRNA3Lys as template. This result indicates that the nature of nucleic acid bound to tRNA3Lys determines which strand of the RNA-tRNA3Lys and DNA-tRNA3Lys hybrids is extended by HIV-1 RT. When an oligoribonucleotide is annealed to an unmodified transcript of tRNA3Lys, both nucleic acids are extended by HIV-1 RT, indicating that specific selection of tRNA3Lys as primer requires the post-transcriptional modifications of tRNA3Lys.},
note = {0022-2836
Journal Article},
keywords = {Base Sequence DNA, Lys/genetics/*metabolism RNA, MARQUET, Non-U.S. Gov't Support, P.H.S., Post-Transcriptional RNA, Transfer, U.S. Gov't, Unité ARN, Viral/genetics HIV-1/*enzymology/genetics HIV-1 Reverse Transcriptase Human Molecular Sequence Data *RNA Processing, Viral/genetics RNA-Directed DNA Polymerase/genetics/*metabolism Support},
pubstate = {published},
tppubtype = {article}
}
1995
Dirheimer G, Baranowski W, Keith G
Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading Journal Article
In: Biochimie, vol. 77, no. 1-2, pp. 99-103, 1995, ISBN: 7599283, (0300-9084 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support
@article{,
title = {Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading},
author = {G Dirheimer and W Baranowski and G Keith},
editor = {Editor},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7599283},
isbn = {7599283},
year = {1995},
date = {1995-01-01},
journal = {Biochimie},
volume = {77},
number = {1-2},
pages = {99-103},
abstract = {Literature references dealing with the variations in the modification level of nucleosides in total eukaryotic tRNAs as a function of different physiological status and after drug administration as well as in sequenced cytoplasmic tRNAs between normal and tumor cells and in SV40-transformed cells are reviewed. In addition, special attention is given to guanine replacement of queuine in the first position of the anticodon of tRNAs. A correlation between the level of this undermodification in cancer tissues and the malignancy grading could be found in human ovarian tumors, confirming the results reported in several laboratories for lymphomas and lung cancer tissues. Indeed tRNAs from primary and metastatic human ovarian malignant tumors are Q deficient as compared to tRNAs from normal tissues or benign tumors: thus queuine deficiency increases with malignancy and grading of differentiation.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support},
pubstate = {published},
tppubtype = {article}
}
Dirheimer G, Baranowski W, Keith G
Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading Journal Article
In: Biochimie, vol. 77, no. 1-2, pp. 99-103, 1995, ISBN: 7599283, (0300-9084 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support
@article{,
title = {Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading},
author = {G Dirheimer and W Baranowski and G Keith},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7599283},
isbn = {7599283},
year = {1995},
date = {1995-01-01},
journal = {Biochimie},
volume = {77},
number = {1-2},
pages = {99-103},
abstract = {Literature references dealing with the variations in the modification level of nucleosides in total eukaryotic tRNAs as a function of different physiological status and after drug administration as well as in sequenced cytoplasmic tRNAs between normal and tumor cells and in SV40-transformed cells are reviewed. In addition, special attention is given to guanine replacement of queuine in the first position of the anticodon of tRNAs. A correlation between the level of this undermodification in cancer tissues and the malignancy grading could be found in human ovarian tumors, confirming the results reported in several laboratories for lymphomas and lung cancer tissues. Indeed tRNAs from primary and metastatic human ovarian malignant tumors are Q deficient as compared to tRNAs from normal tissues or benign tumors: thus queuine deficiency increases with malignancy and grading of differentiation.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support},
pubstate = {published},
tppubtype = {article}
}
Dirheimer G, Baranowski W, Keith G
Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading Journal Article
In: Biochimie, vol. 77, no. 1-2, pp. 99-103, 1995, ISBN: 7599283, (0300-9084 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support, Unité ARN
@article{,
title = {Variations in tRNA modifications, particularly of their queuine content in higher eukaryotes. Its relation to malignancy grading},
author = {G Dirheimer and W Baranowski and G Keith},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7599283},
isbn = {7599283},
year = {1995},
date = {1995-01-01},
journal = {Biochimie},
volume = {77},
number = {1-2},
pages = {99-103},
abstract = {Literature references dealing with the variations in the modification level of nucleosides in total eukaryotic tRNAs as a function of different physiological status and after drug administration as well as in sequenced cytoplasmic tRNAs between normal and tumor cells and in SV40-transformed cells are reviewed. In addition, special attention is given to guanine replacement of queuine in the first position of the anticodon of tRNAs. A correlation between the level of this undermodification in cancer tissues and the malignancy grading could be found in human ovarian tumors, confirming the results reported in several laboratories for lymphomas and lung cancer tissues. Indeed tRNAs from primary and metastatic human ovarian malignant tumors are Q deficient as compared to tRNAs from normal tissues or benign tumors: thus queuine deficiency increases with malignancy and grading of differentiation.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Animals Cell Transformation, Neoplastic/genetics Female Guanine/*analogs & derivatives/analysis Human Neoplasms/*genetics/pathology Ovarian Neoplasms/*genetics/pathology Purines/analysis Pyrimidines/analysis RNA Processing, Non-U.S. Gov't, Post-Transcriptional RNA, Transfer/*chemistry/metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}