Publications
1992
Przykorska A, el Adlouni C, Keith G, Szarkowski J W, Dirheimer G
Structural specificity of Rn nuclease I as probed on yeast tRNA(Phe) and tRNA(Asp) Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 4, p. 659-663, 1992, ISBN: 1542562, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/*metabolism RNA, Base Composition Base Sequence Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't Yeasts/genetics, Pancreatic/*metabolism Secale cereale Substrate Specificity Support, Phe/chemistry/genetics/*metabolism Ribonuclease, Transfer, Unité ARN
@article{,
title = {Structural specificity of Rn nuclease I as probed on yeast tRNA(Phe) and tRNA(Asp)},
author = {A Przykorska and C el Adlouni and G Keith and J W Szarkowski and G Dirheimer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1542562},
isbn = {1542562},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {4},
pages = {659-663},
abstract = {A single-strand-specific nuclease from rye germ (Rn nuclease I) was characterized as a tool for secondary and tertiary structure investigation of RNAs. To test the procedure, yeast tRNA(Phe) and tRNA(Asp) for which the tertiary structures are known, as well as the 3'-half of tRNA(Asp) were used as substrates. In tRNA(Phe) the nuclease introduced main primary cuts at positions U33 and A35 of the anticodon loop and G18 and G19 of the D loop. No primary cuts were observed within the double stranded stems. In tRNA(Asp) the main cuts occurred at positions U33, G34, U35, C36 of the anticodon loop and G18 and C20:1 positions in the D loop. No cuts were observed in the T loop in intact tRNA(Asp) but strong primary cleavages occurred at positions psi 55, C56, A57 within that loop in the absence of the tertiary interactions between T and D loops (use of 3'-half tRNA(Asp)). These results show that Rn nuclease I is specific for exposed single-stranded regions.},
note = {0305-1048
Journal Article},
keywords = {Asp/chemistry/genetics/*metabolism RNA, Base Composition Base Sequence Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't Yeasts/genetics, Pancreatic/*metabolism Secale cereale Substrate Specificity Support, Phe/chemistry/genetics/*metabolism Ribonuclease, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Perret V, Florentz C, Puglisi J D, Giege R
Effect of conformational features on the aminoacylation of tRNAs and consequences on the permutation of tRNA specificities Article de journal
Dans: J Mol Biol, vol. 226, no. 2, p. 323-333, 1992, ISBN: 1640453, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Activation Aspartate-tRNA Ligase/*metabolism Base Sequence Molecular Sequence Data Nucleic Acid Conformation Phenylalanine-tRNA Ligase/*metabolism RNA, Asp/metabolism/*ultrastructure RNA, FLORENTZ, Fungal/metabolism/ultrastructure RNA, Non-U.S. Gov't, Phe/metabolism/*ultrastructure Saccharomyces cerevisiae Structure-Activity Relationship Substrate Specificity Support, Transfer, Unité ARN
@article{,
title = {Effect of conformational features on the aminoacylation of tRNAs and consequences on the permutation of tRNA specificities},
author = {V Perret and C Florentz and J D Puglisi and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1640453},
isbn = {1640453},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {226},
number = {2},
pages = {323-333},
abstract = {The structure and function of in vitro transcribed tRNA(Asp) variants with inserted conformational features characteristic of yeast tRNA(Phe), such as the length of the variable region or the arrangement of the conserved residues in the D-loop, have been investigated. Although they exhibit significant conformational alterations as revealed by Pb2+ treatment, these variants are still efficiently aspartylated by yeast aspartyl-tRNA synthetase. Thus, this synthetase can accommodate a variety of tRNA conformers. In a second series of variants, the identity determinants of yeast tRNA(Phe) were transplanted into the previous structural variants of tRNA(Asp). The phenylalanine acceptance of these variants improves with increasing the number of structural characteristics of tRNA(Phe), suggesting that phenylalanyl-tRNA synthetase is sensitive to the conformational frame embedding the cognate identity nucleotides. These results contrast with the efficient transplantation of tRNA(Asp) identity elements into yeast tRNA(Phe). This indicates that synthetases respond differently to the detailed conformation of their tRNA substrates. Efficient aminoacylation is not only dependent on the presence of the set of identity nucleotides, but also on a precise conformation of the tRNA.},
note = {0022-2836
Journal Article},
keywords = {Amino Acid Activation Aspartate-tRNA Ligase/*metabolism Base Sequence Molecular Sequence Data Nucleic Acid Conformation Phenylalanine-tRNA Ligase/*metabolism RNA, Asp/metabolism/*ultrastructure RNA, FLORENTZ, Fungal/metabolism/ultrastructure RNA, Non-U.S. Gov't, Phe/metabolism/*ultrastructure Saccharomyces cerevisiae Structure-Activity Relationship Substrate Specificity Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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) Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 8, p. 1959-1965, 1992, ISBN: 1579498, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Animals Base Sequence Blotting, Gel, Lys/*analysis/metabolism Ribonucleoproteins/*chemistry/drug effects Support, Non-U.S. Gov't Zinc/pharmacology, Northern Ducks Electrophoresis, Transfer, Two-Dimensional Erythroblasts Hela Cells Human Molecular Sequence Data RNA Nucleotidyltransferases/metabolism RNA, Unité ARN
@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},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1579498},
isbn = {1579498},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {8},
pages = {1959-1965},
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 Sequence Blotting, Gel, Lys/*analysis/metabolism Ribonucleoproteins/*chemistry/drug effects Support, Non-U.S. Gov't Zinc/pharmacology, Northern Ducks Electrophoresis, Transfer, Two-Dimensional Erythroblasts Hela Cells Human Molecular Sequence Data RNA Nucleotidyltransferases/metabolism RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Myslinski E, Krol A, Carbon P
Optimal tRNA((Ser)Sec) gene activity requires an upstream SPH motif Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 2, p. 203-209, 1992, ISBN: 1311068, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid-Specific/*genetics Recombinant Fusion Proteins/genetics/metabolism Simian virus 40/*genetics Support, Animals Base Sequence DNA Mutational Analysis DNA-Binding Proteins/genetics Enhancer Elements (Genetics)/*genetics/physiology Gene Expression Regulation/*genetics Molecular Sequence Data Promoter Regions (Genetics)/genetics RNA, Non-U.S. Gov't TATA Box/genetics Xenopus laevis/*genetics, Small Nuclear/genetics RNA, Transfer, Unité ARN
@article{,
title = {Optimal tRNA((Ser)Sec) gene activity requires an upstream SPH motif},
author = {E Myslinski and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1311068},
isbn = {1311068},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {2},
pages = {203-209},
abstract = {The X. laevis tRNA((Ser)Sec) gene is different from the other tRNA genes in that its promoter contains two external elements, a PSE and a TATA box functionally equivalent to those of the U6 snRNA gene. Of the two internal promoters governing classical tRNA gene transcription, only subsists the internal B box. In this report, we show that the tRNA((Ser)Sec) contains in addition an activator element (AE) which we have mapped by extensive mutagenesis. Activation is only dependent on a 15 bp fragment residing between -209 and -195 and containing an SPH motif. In vitro, this element forms a complex with a nuclear protein which is different from the TEF-1 transcriptional activator that binds the SV40 Sph motifs. This AE is versatile since it shows capacity of activating a variety of genes in vivo, including U1 and U6 snRNAs and HSV thymidine kinase. Unexpectedly for an snRNA-related gene, the tRNA((Ser)Sec) is deprived of octamer or octamer-like motifs. The X.laevis tRNA((Ser)Sec) gene represents the first example of a Pol III snRNA-type gene whose activation of transcription is completely octamer-independent.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid-Specific/*genetics Recombinant Fusion Proteins/genetics/metabolism Simian virus 40/*genetics Support, Animals Base Sequence DNA Mutational Analysis DNA-Binding Proteins/genetics Enhancer Elements (Genetics)/*genetics/physiology Gene Expression Regulation/*genetics Molecular Sequence Data Promoter Regions (Genetics)/genetics RNA, Non-U.S. Gov't TATA Box/genetics Xenopus laevis/*genetics, Small Nuclear/genetics RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Heitzler J, Marechal-Drouard L, Dirheimer G, Keith G
Use of a dot blot hybridization method for identification of pure tRNA species on different membranes Article de journal
Dans: Biochim Biophys Acta-Gene Regul Mech, vol. 1129, no. 3, p. 273-277, 1992, ISBN: 1536878, (0006-3002 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Artificial Nucleic Acid Hybridization RNA, Autoradiography *Membranes, Fungal/genetics RNA, Met/genetics Saccharomyces cerevisiae/genetics Support, Non-U.S. Gov't, Transfer, Transfer/*genetics RNA, Unité ARN
@article{,
title = {Use of a dot blot hybridization method for identification of pure tRNA species on different membranes},
author = {J Heitzler and L Marechal-Drouard and G Dirheimer and G Keith},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1536878},
isbn = {1536878},
year = {1992},
date = {1992-01-01},
journal = {Biochim Biophys Acta-Gene Regul Mech},
volume = {1129},
number = {3},
pages = {273-277},
abstract = {The characterization of a tRNA in purification procedures usually involves aminoacylation assays but recently, the hybridization by dot blot with specific oligonucleotides as probes has been used for the tRNA identification. We present here an optimization of a dot blot hybridization method for the tRNA detection by comparing the efficiency of eight different nylon membranes. Neutral 0.22 microns porosity membranes (Nytran, Biodine A) give the best detection efficiency when small quantities of material (less than 40 ng of tRNA) are dotted on filter; by contrast, neutral 0.45 microns porosity membranes (such as Hybond N) are the most efficient when larger quantities of tRNA are dotted on the filter. The described technique allows to detect less than 20 pg of a pure tRNA species. Its use in the identification of Saccharomyces cerevisiae initiator tRNA(Met) in counter-current distribution fractions is shown.},
note = {0006-3002
Journal Article},
keywords = {Artificial Nucleic Acid Hybridization RNA, Autoradiography *Membranes, Fungal/genetics RNA, Met/genetics Saccharomyces cerevisiae/genetics Support, Non-U.S. Gov't, Transfer, Transfer/*genetics RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Graffe M, Dondon J, Caillet J, Romby P, Ehresmann C, Ehresmann B, Springer M
The specificity of translational control switched with transfer RNA identity rules Article de journal
Dans: Science, vol. 255, no. 5047, p. 994-996, 1992, ISBN: 1372129, (0036-8075 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN
@article{,
title = {The specificity of translational control switched with transfer RNA identity rules},
author = {M Graffe and J Dondon and J Caillet and P Romby and C Ehresmann and B Ehresmann and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1372129},
isbn = {1372129},
year = {1992},
date = {1992-01-01},
journal = {Science},
volume = {255},
number = {5047},
pages = {994-996},
abstract = {The interaction of Escherichia coli threonyl-transfer RNA (tRNA) synthetase with the leader sequence of its own messenger RNA inhibits ribosome binding, resulting in negative translational feedback regulation. The leader sequence resembles the substrate (tRNA(Thr)) of the enzyme, and the nucleotides that mediate the correct recognition of the leader and the tRNA may be the same. A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to tRNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNA synthetase. This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs.},
note = {0036-8075
Journal Article},
keywords = {Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Glasser A L, el Adlouni C, Keith G, Sochacka E, Malkiewicz A, Santos M, Tuite M F, Desgres J
Presence and coding properties of 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um) in the wobble position of the anticodon of tRNA(Leu) (U*AA) from brewer's yeast Article de journal
Dans: FEBS Lett, vol. 314, no. 3, p. 381-385, 1992, ISBN: 1468572, (0014-5793 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: *Anticodon Chromatography, Fungal/genetics RNA, High Pressure Liquid Fungal Proteins/biosynthesis Molecular Structure RNA, Leu/*genetics Saccharomyces cerevisiae/*genetics Spectrophotometry, Mass Support, Non-U.S. Gov't Uridine/*analogs & derivatives/analysis/chemistry/genetics, Transfer, Ultraviolet Spectrum Analysis, Unité ARN
@article{,
title = {Presence and coding properties of 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um) in the wobble position of the anticodon of tRNA(Leu) (U*AA) from brewer's yeast},
author = {A L Glasser and C el Adlouni and G Keith and E Sochacka and A Malkiewicz and M Santos and M F Tuite and J Desgres},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1468572},
isbn = {1468572},
year = {1992},
date = {1992-01-01},
journal = {FEBS Lett},
volume = {314},
number = {3},
pages = {381-385},
abstract = {The unknown modified nucleoside U* has been isolated by enzymatic and HPLC protocols from tRNA(Leu) (U*AA) recently discovered in brewer's yeast. The pure U* nucleoside has been characterized by electron impact mass spectroscopy, and comparison of its chromatographic and UV-absorption properties with those of appropriate synthetic compounds. The structure of U* was established as 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um). The yeast tRNA(Leu) (U*AA) is the only tRNA so far sequenced which has been shown to contain ncm5Um. The location of such a modified uridine at the first position of the anticodon restricts the decoding property to A of the leucine UUA codon.},
note = {0014-5793
Journal Article},
keywords = {*Anticodon Chromatography, Fungal/genetics RNA, High Pressure Liquid Fungal Proteins/biosynthesis Molecular Structure RNA, Leu/*genetics Saccharomyces cerevisiae/*genetics Spectrophotometry, Mass Support, Non-U.S. Gov't Uridine/*analogs & derivatives/analysis/chemistry/genetics, Transfer, Ultraviolet Spectrum Analysis, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Garcia A, Giege R
Footprinting evidence for close contacts of the yeast tRNA(Asp) anticodon region with aspartyl-tRNA synthetase Article de journal
Dans: Biochem Biophys Res Commun, vol. 186, no. 2, p. 956-962, 1992, ISBN: 1497679, (0006-291x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Alkylation Anticodon/*metabolism Aspartate-tRNA Ligase/*metabolism Base Sequence Molecular Sequence Data Nucleic Acid Conformation Protein Binding RNA, Asp/genetics/isolation & purification/*metabolism Saccharomyces cerevisiae/enzymology/*genetics Sulfuric Acid Esters/metabolism/pharmacology Support, Non-U.S. Gov't, Transfer, Unité ARN
@article{,
title = {Footprinting evidence for close contacts of the yeast tRNA(Asp) anticodon region with aspartyl-tRNA synthetase},
author = {A Garcia and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1497679},
isbn = {1497679},
year = {1992},
date = {1992-01-01},
journal = {Biochem Biophys Res Commun},
volume = {186},
number = {2},
pages = {956-962},
abstract = {Chemical footprinting experiments on brewer's yeast tRNA(Asp) complexed to its cognate aspartyl-tRNA synthetase are reported: they demonstrate that bases of the anticodon loop, including the anticodon itself, are in close proximity with the synthetase. Contacts were determined using dimethylsulfate as the probe for testing reactivity of guanine and cytosine residues in free and complexed tRNA. Results correlate with the decrease in aspartylation activity of yeast tRNA(Asp) molecules mutated at these contact positions and will be compared with other structural data arising from solution and crystallographic studies on the aspartic acid complex.},
note = {0006-291x
Journal Article},
keywords = {Alkylation Anticodon/*metabolism Aspartate-tRNA Ligase/*metabolism Base Sequence Molecular Sequence Data Nucleic Acid Conformation Protein Binding RNA, Asp/genetics/isolation & purification/*metabolism Saccharomyces cerevisiae/enzymology/*genetics Sulfuric Acid Esters/metabolism/pharmacology Support, Non-U.S. Gov't, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Frugier M, Florentz C, Giege R
Anticodon-independent aminoacylation of an RNA minihelix with valine Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 89, no. 9, p. 3990-3994, 1992, ISBN: 1570324, (0027-8424 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: *Amino Acid Activation Anticodon Base Sequence Hydrogen Bonding In Vitro Molecular Sequence Data RNA, ERIANI, FLORENTZ, FRUGIER, Non-U.S. Gov't Valine-tRNA Ligase/*metabolism, Transfer, Unité ARN, Val/chemistry/*metabolism Saccharomyces cerevisiae Structure-Activity Relationship Support
@article{,
title = {Anticodon-independent aminoacylation of an RNA minihelix with valine},
author = {M Frugier and C Florentz and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1570324},
isbn = {1570324},
year = {1992},
date = {1992-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {89},
number = {9},
pages = {3990-3994},
abstract = {Minihelices mimicking the amino acid acceptor and anticodon branches of yeast tRNA(Val) have been synthesized by in vitro transcription of synthetic templates. It is shown that a minihelix corresponding to the amino acid acceptor branch and containing solely a valine-specific identity nucleotide can be aminoacylated by yeast valyl-tRNA synthetase. Its charging ability is lost after mutating this nucleotide. This ability is stimulated somewhat by the addition of a second hairpin helix that mimicks the anticodon arm, which suggests that information originating from the anticodon stem-loop can be transmitted to the active site of the enzyme by the core of the protein.},
note = {0027-8424
Journal Article},
keywords = {*Amino Acid Activation Anticodon Base Sequence Hydrogen Bonding In Vitro Molecular Sequence Data RNA, ERIANI, FLORENTZ, FRUGIER, Non-U.S. Gov't Valine-tRNA Ligase/*metabolism, Transfer, Unité ARN, Val/chemistry/*metabolism Saccharomyces cerevisiae Structure-Activity Relationship Support},
pubstate = {published},
tppubtype = {article}
}
Eiler S, Boeglin M, Martin F, Eriani G, Gangloff J, Thierry J C, Moras D
Crystallization of aspartyl-tRNA synthetase-tRNA(Asp) complex from Escherichia coli and first crystallographic results Article de journal
Dans: J Mol Biol, vol. 224, no. 4, p. 1171-1173, 1992, ISBN: 1569573, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/*ultrastructure X-Ray Diffraction, Aspartate-tRNA Ligase/*ultrastructure Crystallography Escherichia coli/enzymology RNA, ERIANI, Transfer, Unité ARN
@article{,
title = {Crystallization of aspartyl-tRNA synthetase-tRNA(Asp) complex from Escherichia coli and first crystallographic results},
author = {S Eiler and M Boeglin and F Martin and G Eriani and J Gangloff and J C Thierry and D Moras},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1569573},
isbn = {1569573},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {224},
number = {4},
pages = {1171-1173},
abstract = {Crystals of the dimeric aspartyl-tRNA synthetase from Escherichia coli (molecular mass 132,000 Da) complexed with its cognate tRNA (molecular mass 25,000 Da) have been grown using ammonium sulfate as precipitant. The crystals belong to the orthorhombic space group C222(1) with unit cell parameters a = 102.75 A},
note = {0022-2836
Journal Article},
keywords = {Asp/*ultrastructure X-Ray Diffraction, Aspartate-tRNA Ligase/*ultrastructure Crystallography Escherichia coli/enzymology RNA, ERIANI, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Despons L, Senger B, Fasiolo F, Walter P
Binding of the yeast tRNA(Met) anticodon by the cognate methionyl-tRNA synthetase involves at least two independent peptide regions Article de journal
Dans: J Mol Biol, vol. 225, no. 3, p. 897-907, 1992, ISBN: 1602489, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Anticodon/*metabolism Binding Sites Kinetics Methionine-tRNA Ligase/*metabolism Models, Met/*metabolism Saccharomyces cerevisiae/enzymology Structure-Activity Relationship Support, Molecular Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Site-Directed Protein Conformation RNA, Transfer, Unité ARN
@article{,
title = {Binding of the yeast tRNA(Met) anticodon by the cognate methionyl-tRNA synthetase involves at least two independent peptide regions},
author = {L Despons and B Senger and F Fasiolo and P Walter},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1602489},
isbn = {1602489},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {225},
number = {3},
pages = {897-907},
abstract = {As for Escherichia coli methionine tRNAs, the anticodon triplet of yeast tRNA(Met) plays an important role in the recognition by the yeast methionyl-tRNA synthetase (MetRS), indicating that this determinant for methionine identity is conserved in yeast. Efficient aminoacylation of the E. coli tRNA(Met) transcript by the heterologous yeast methionine enzyme also suggests conservation of the protein determinants that interact with the CAU anticodon sequence. We have analysed by site-directed mutagenesis the peptide region 655 to 663 of the yeast MetRS that is equivalent to the anticodon binding region of the E. coli methionine enzyme. Only one change, converting Leu658 into Ala significantly reduced tRNA aminoacylation. Semi-conservative substitutions of L658 allow a correlation to be drawn between side-chain volume of the hydrophobic residue at this site and activity. The analysis of the L658A mutant shows that Km is mainly affected. This suggests that the peptide region 655 to 663 contributes partially to the binding of the anticodon, since separate mutational analysis of the anticodon bases shows that kcat is the most critical parameter in the recognition of tRNA(Met) by the yeast synthetase. We have analysed the role of peptide region (583-GNLVNR-588) that is spatially close to the region 655 to 663. Replacements of residues N584 and R588 reduces significantly the kcat of aminoacylation. The peptide region 583-GNLVNR-588 is highly conserved in all MetRS so far sequenced. We therefore propose that the hydrogen donor/acceptor amino acid residues within this region are the most critical protein determinants for the positive selection of the methionine tRNAs.},
note = {0022-2836
Journal Article},
keywords = {Amino Acid Sequence Anticodon/*metabolism Binding Sites Kinetics Methionine-tRNA Ligase/*metabolism Models, Met/*metabolism Saccharomyces cerevisiae/enzymology Structure-Activity Relationship Support, Molecular Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Site-Directed Protein Conformation RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Brunel C, Caillet J, Lesage P, Graffe M, Dondon J, Moine H, Romby P, Ehresmann C, Ehresmann B, Grunberg-Manago M, Springer M
Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors Article de journal
Dans: J Mol Biol, vol. 227, no. 3, p. 621-634, 1992, ISBN: 1383551, (0022-2836).
Résumé | Liens | BibTeX | Étiquettes: Bacterial/genetics Gene Expression Regulation, Bacterial/genetics RNA, Base Sequence Escherichia coli/genetics Gene Expression Regulation, Enzymologic/*genetics Molecular Sequence Data Mutagenesis, Genetic/*genetics, Messenger/*genetics/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism Translation, ROMBY, Site-Directed/genetics Nucleic Acid Conformation RNA, Thr/*genetics/metabolism Recombinant Fusion Proteins/genetics Support, Transfer, Unité ARN
@article{,
title = {Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors},
author = {C Brunel and J Caillet and P Lesage and M Graffe and J Dondon and H Moine and P Romby and C Ehresmann and B Ehresmann and M Grunberg-Manago and M Springer},
url = {http://www.ncbi.nlm.nih.gov/pubmed/1383551},
doi = {10.1016/0022-2836(92)90212-3},
isbn = {1383551},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {227},
number = {3},
pages = {621-634},
abstract = {The expression of the gene for threonyl-tRNA synthetase (thrS) is negatively autoregulated at the translational level in Escherichia coli. The synthetase binds to a region of the thrS leader mRNA upstream from the ribosomal binding site inhibiting subsequent translation. The leader mRNA consists of four structural domains. The present work shows that mutations in these four domains affect expression and/or regulation in different ways. Domain 1, the 3' end of the leader, contains the ribosomal binding site, which appears not to be essential for synthetase binding. Mutations in this domain probably affect regulation by changing the competition between the ribosome and the synthetase for binding to the leader. Domain 2, 3' from the ribosomal binding site, is a stem and loop with structural similarities to the tRNA(Thr) anticodon arm. In tRNAs the anticodon loop is seven nucleotides long, mutations that increase or decrease the length of the anticodon-like loop of domain 2 from seven nucleotides abolish control. The nucleotides in the second and third positions of the anticodon-like sequence are essential for recognition and the nucleotide in the wobble position is not, again like tRNA(Thr). The effect of mutations in domain 3 indicate that it acts as an articulation between domains 2 and 4. Domain 4 is a stable arm that has similarities to the acceptor arm of tRNA(Thr) and is shown to be necessary for regulation. Based on this mutational analysis and previous footprinting experiments, it appears that domains 2 and 4, those analogous to tRNA(Thr), are involved in binding the synthetase which inhibits translation probably by interfering with ribosome loading at the nearby translation initiation site.},
note = {0022-2836},
keywords = {Bacterial/genetics Gene Expression Regulation, Bacterial/genetics RNA, Base Sequence Escherichia coli/genetics Gene Expression Regulation, Enzymologic/*genetics Molecular Sequence Data Mutagenesis, Genetic/*genetics, Messenger/*genetics/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism Translation, ROMBY, Site-Directed/genetics Nucleic Acid Conformation RNA, Thr/*genetics/metabolism Recombinant Fusion Proteins/genetics Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}