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 Article de journal
Dans: Mol Cell, vol. 8, no. 6, p. 1363-1373, 2001, ISBN: 11779510, (1097-2765 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 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}
}
Wittberger D, Berens C, Hammann C, Westhof E, Schroeder R
Evaluation of uranyl photocleavage as a probe to monitor ion binding and flexibility in RNAs Article de journal
Dans: J Mol Biol, vol. 300, no. 2, p. 339-352, 2000, ISBN: 10873469, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Animals Base Pairing Base Sequence Ethylnitrosourea/metabolism Hepatitis Delta Virus/genetics Hydrogen Peroxide/metabolism Introns/genetics Ions/metabolism Iron/metabolism Lead/metabolism Magnesium Chloride/pharmacology Models, Asp/chemistry/genetics/metabolism RNA, Catalytic/chemistry/genetics/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation *Photolysis/drug effects Pliability RNA/*chemistry/genetics/*metabolism RNA, Non-U.S. Gov't Tetrahymena/genetics Uranyl Nitrate/*metabolism Yeasts/genetics, Phe/chemistry/genetics/metabolism RNA, Protozoan/chemistry/genetics/metabolism RNA, Transfer, Unité ARN, Viral/chemistry/genetics/metabolism Solvents Support
@article{,
title = {Evaluation of uranyl photocleavage as a probe to monitor ion binding and flexibility in RNAs},
author = {D Wittberger and C Berens and C Hammann and E Westhof and R Schroeder},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10873469},
isbn = {10873469},
year = {2000},
date = {2000-01-01},
journal = {J Mol Biol},
volume = {300},
number = {2},
pages = {339-352},
abstract = {In order to evaluate uranyl photocleavage as a tool to identify and characterize structural and dynamic properties in RNA, we compared uranyl cleavage sites in five RNA molecules with known X-ray structures, namely the hammerhead and hepatitis delta virus ribozymes, the P4-P6 domain of the Tetrahymena group I intron, as well as tRNA(Phe) and tRNA(Asp) from yeast. Uranyl photocleavage was observed at specific positions in all molecules investigated. In order to characterize the sites, photocleavage was performed in the absence and in increasing amounts of MgCl(2). Uranyl photocleavage correlates well with sites of low calculated accessibility, suggesting that uranyl ions bind in tight RNA pockets formed by close approach of phosphate groups. RNA foldings require ion binding, usually magnesium ions. Thus, upon the adoption of the native structure, uranyl ions can no longer bind well except in flexible and open to the solvent regions that can undergo induced-fit without disrupting the native fold. Uranyl photocleavage was compared to N-ethyl-N-nitrosourea and lead-induced cleavages in the context of the three-dimensional X-ray structures. Overall, the regions protected from ENU attack are sites of uranyl cleavage, indicating sites of low accessibility which can form ion binding sites. On the contrary, lead cleavages occur at flexible and accessible sites and correlate with the unspecific cleavages prevalent in dynamic and open regions. Applied in a magnesium-dependent manner, and only in combination with other backbone probing agents such as N-ethyl-N-nitrosourea, lead and Fenton cleavage, uranyl probing has the potential to reveal high-affinity metal ion environments, as well as regions involved in conformational transitions.},
note = {0022-2836
Journal Article},
keywords = {Animals Base Pairing Base Sequence Ethylnitrosourea/metabolism Hepatitis Delta Virus/genetics Hydrogen Peroxide/metabolism Introns/genetics Ions/metabolism Iron/metabolism Lead/metabolism Magnesium Chloride/pharmacology Models, Asp/chemistry/genetics/metabolism RNA, Catalytic/chemistry/genetics/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation *Photolysis/drug effects Pliability RNA/*chemistry/genetics/*metabolism RNA, Non-U.S. Gov't Tetrahymena/genetics Uranyl Nitrate/*metabolism Yeasts/genetics, Phe/chemistry/genetics/metabolism RNA, Protozoan/chemistry/genetics/metabolism RNA, Transfer, Unité ARN, Viral/chemistry/genetics/metabolism Solvents Support},
pubstate = {published},
tppubtype = {article}
}
Sauter C, Lorber B, Cavarelli J, Moras D, Giege R
The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain Article de journal
Dans: J Mol Biol, vol. 299, no. 5, p. 1313-1324, 2000, ISBN: 10873455, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/chemistry/genetics/*metabolism Aspartate-tRNA Ligase/*chemistry/genetics/*metabolism Binding Sites Catalytic Domain Conserved Sequence/genetics Crystallization Crystallography, Asp/chemistry/genetics/*metabolism Rotation Sequence Deletion/genetics Support, Fungal/chemistry/genetics/metabolism RNA, Molecular Molecular Sequence Data Movement Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Yeasts/*enzymology/genetics, SAUTER, Secondary RNA, Transfer, Unité ARN, X-Ray Models
@article{,
title = {The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain},
author = {C Sauter and B Lorber and J Cavarelli and D Moras and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10873455},
isbn = {10873455},
year = {2000},
date = {2000-01-01},
journal = {J Mol Biol},
volume = {299},
number = {5},
pages = {1313-1324},
abstract = {Aminoacyl-tRNA synthetases catalyze the specific charging of amino acid residues on tRNAs. Accurate recognition of a tRNA by its synthetase is achieved through sequence and structural signalling. It has been shown that tRNAs undergo large conformational changes upon binding to enzymes, but little is known about the conformational rearrangements in tRNA-bound synthetases. To address this issue the crystal structure of the dimeric class II aspartyl-tRNA synthetase (AspRS) from yeast was solved in its free form and compared to that of the protein associated to the cognate tRNA(Asp). The use of an enzyme truncated in N terminus improved the crystal quality and allowed us to solve and refine the structure of free AspRS at 2.3 A resolution. For the first time, snapshots are available for the different macromolecular states belonging to the same tRNA aminoacylation system, comprising the free forms for tRNA and enzyme, and their complex. Overall, the synthetase is less affected by the association than the tRNA, although significant local changes occur. They concern a rotation of the anticodon binding domain and a movement in the hinge region which connects the anticodon binding and active-site domains in the AspRS subunit. The most dramatic differences are observed in two evolutionary conserved loops. Both are in the neighborhood of the catalytic site and are of importance for ligand binding. The combination of this structural analysis with mutagenesis and enzymology data points to a tRNA binding process that starts by a recognition event between the tRNA anticodon loop and the synthetase anticodon binding module.},
note = {0022-2836
Journal Article},
keywords = {Anticodon/chemistry/genetics/*metabolism Aspartate-tRNA Ligase/*chemistry/genetics/*metabolism Binding Sites Catalytic Domain Conserved Sequence/genetics Crystallization Crystallography, Asp/chemistry/genetics/*metabolism Rotation Sequence Deletion/genetics Support, Fungal/chemistry/genetics/metabolism RNA, Molecular Molecular Sequence Data Movement Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Yeasts/*enzymology/genetics, SAUTER, Secondary RNA, Transfer, Unité ARN, X-Ray Models},
pubstate = {published},
tppubtype = {article}
}
Perreau V M, Keith G, Holmes W M, Przykorska A, Santos M A, Tuite M F
The Candida albicans CUG-decoding ser-tRNA has an atypical anticodon stem-loop structure Article de journal
Dans: J Mol Biol, vol. 293, no. 5, p. 1039-1053, 1999, ISBN: 10547284, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/*chemistry/*genetics/metabolism Base Sequence Candida albicans/*genetics Evolution, Fungal/chemistry/genetics/metabolism RNA, Molecular Genetic Code/genetics Imidazoles/metabolism Lead/metabolism Methylation Mutation/genetics *Nucleic Acid Conformation Nucleosides/genetics/metabolism RNA, Non-P.H.S. Support, Non-U.S. Gov't Support, P.H.S. tRNA Methyltransferases/metabolism, Ser/*chemistry/*genetics/metabolism Ribonucleases/metabolism Saccharomyces cerevisiae/genetics Solutions Support, Transfer, U.S. Gov't, Unité ARN
@article{,
title = {The Candida albicans CUG-decoding ser-tRNA has an atypical anticodon stem-loop structure},
author = {V M Perreau and G Keith and W M Holmes and A Przykorska and M A Santos and M F Tuite},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10547284},
isbn = {10547284},
year = {1999},
date = {1999-01-01},
journal = {J Mol Biol},
volume = {293},
number = {5},
pages = {1039-1053},
abstract = {In many Candida species, the leucine CUG codon is decoded by a tRNA with two unusual properties: it is a ser-tRNA and, uniquely, has guanosine at position 33 (G33). Using a combination of enzymatic (V1 RNase, RnI nuclease) and chemical (Pb(2+), imidazole) probing of the native Candida albicans ser-tRNACAG, we demonstrate that the overall tertiary structure of this tRNA resembles that of a ser-tRNA rather than a leu-tRNA, except within the anticodon arm where there is considerable disruption of the anticodon stem. Using non-modified in vitro transcripts of the C. albicans ser-tRNACAG carrying G, C, U or A at position 33, we demonstrate that it is specifically a G residue at this position that induces the atypical anticodon stem structure. Further quantitative evidence for an unusual structure in the anticodon arm of the G33-tRNA is provided by the observed change in kinetics of methylation of the G at position 37, by purified Escherichia coli m(1)G37 methyltransferase. We conclude that the anticodon arm distortion, induced by a guanosine base at position 33 in the anticodon loop of this novel tRNA, results in reduced decoding ability which has facilitated the evolution of this tRNA without extinction of the species encoding it.},
note = {0022-2836
Journal Article},
keywords = {Anticodon/*chemistry/*genetics/metabolism Base Sequence Candida albicans/*genetics Evolution, Fungal/chemistry/genetics/metabolism RNA, Molecular Genetic Code/genetics Imidazoles/metabolism Lead/metabolism Methylation Mutation/genetics *Nucleic Acid Conformation Nucleosides/genetics/metabolism RNA, Non-P.H.S. Support, Non-U.S. Gov't Support, P.H.S. tRNA Methyltransferases/metabolism, Ser/*chemistry/*genetics/metabolism Ribonucleases/metabolism Saccharomyces cerevisiae/genetics Solutions Support, Transfer, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Gabryszuk J, Keith G, Monko M, Kuligowska E, Dirheimer G, Szarkowski J W, Przykorska A
Structural specificity of nuclease from wheat chloroplasts stroma Article de journal
Dans: Nucleic Acids Symp Ser, no. 33, p. 115-9, 1995, ISBN: 8643343, (0261-3166 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer
@article{,
title = {Structural specificity of nuclease from wheat chloroplasts stroma},
author = {J Gabryszuk and G Keith and M Monko and E Kuligowska and G Dirheimer and J W Szarkowski and A Przykorska},
editor = {Editor},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8643343},
isbn = {8643343},
year = {1995},
date = {1995-01-01},
journal = {Nucleic Acids Symp Ser},
number = {33},
pages = {115-9},
abstract = {A single-strand-specific nuclease from wheat chloroplasts (ChS nuclease) was tested as a tool for RNA secondary and tertiary structure investigations, using yeast tRNA(Phe) and yeast tRNA(Asp) as models. In tRNA(Phe) the nuclease introduced main primary cleavages at positions U33, A35 and A36 in the anticodon-loop and G18 and G19 in the D-loop. In tRNA(Asp) the main primary cleavages occurred at positions U33, G34 and U35 in the anticodon-loop and the lower one at position C20:1 in the D-loop. No primary cleavages were observed within the double-stranded stems. Because ChS nuclease has (i) a low molecular weight, (ii) a wide pH range of action (5.0 to 7.5) (iii) no divalent cation requirement in the reaction mixture and (iv) can be obtained as a pure protein in rather large quantities it appeared to be a very good tool for secondary and tertiary structural studies of RNAs.},
note = {0261-3166
Journal Article},
keywords = {Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer},
pubstate = {published},
tppubtype = {article}
}
Gabryszuk J, Keith G, Monko M, Kuligowska E, Dirheimer G, Szarkowski J W, Przykorska A
Structural specificity of nuclease from wheat chloroplasts stroma Article de journal
Dans: Nucleic Acids Symp Ser, no. 33, p. 115-9, 1995, ISBN: 8643343, (0261-3166 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer
@article{,
title = {Structural specificity of nuclease from wheat chloroplasts stroma},
author = {J Gabryszuk and G Keith and M Monko and E Kuligowska and G Dirheimer and J W Szarkowski and A Przykorska},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8643343},
isbn = {8643343},
year = {1995},
date = {1995-01-01},
journal = {Nucleic Acids Symp Ser},
number = {33},
pages = {115-9},
abstract = {A single-strand-specific nuclease from wheat chloroplasts (ChS nuclease) was tested as a tool for RNA secondary and tertiary structure investigations, using yeast tRNA(Phe) and yeast tRNA(Asp) as models. In tRNA(Phe) the nuclease introduced main primary cleavages at positions U33, A35 and A36 in the anticodon-loop and G18 and G19 in the D-loop. In tRNA(Asp) the main primary cleavages occurred at positions U33, G34 and U35 in the anticodon-loop and the lower one at position C20:1 in the D-loop. No primary cleavages were observed within the double-stranded stems. Because ChS nuclease has (i) a low molecular weight, (ii) a wide pH range of action (5.0 to 7.5) (iii) no divalent cation requirement in the reaction mixture and (iv) can be obtained as a pure protein in rather large quantities it appeared to be a very good tool for secondary and tertiary structural studies of RNAs.},
note = {0261-3166
Journal Article},
keywords = {Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer},
pubstate = {published},
tppubtype = {article}
}
Vlassov V V, Zuber G, Felden B, Behr J P, Giege R
Cleavage of tRNA with imidazole and spermine imidazole constructs: a new approach for probing RNA structure Article de journal
Dans: Nucleic Acids Res, vol. 23, no. 16, p. 3161-3167, 1995, ISBN: 7667092, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/*chemistry/genetics/*metabolism RNA, Base Sequence Binding Sites Buffers Hydrolysis Imidazoles Molecular Probes Molecular Sequence Data Molecular Structure Nucleic Acid Conformation RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Tobacco Mosaic Virus/genetics/metabolism, Transfer, Unité ARN, Viral/chemistry/genetics/metabolism Saccharomyces cerevisiae/genetics/metabolism Spermine Support
@article{,
title = {Cleavage of tRNA with imidazole and spermine imidazole constructs: a new approach for probing RNA structure},
author = {V V Vlassov and G Zuber and B Felden and J P Behr and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7667092},
isbn = {7667092},
year = {1995},
date = {1995-01-01},
journal = {Nucleic Acids Res},
volume = {23},
number = {16},
pages = {3161-3167},
abstract = {Hydrolysis of RNA in imidazole buffer and by spermine-imidazole conjugates has been investigated. The RNA models were yeast tRNA(Asp) and a transcript derived from the 3'-terminal sequence of tobacco mosaic virus RNA representing a minihelix capable of being enzymatically aminoacylated with histidine. Imidazole buffer and spermine-imidazole conjugates in the presence of free imidazole cleave phosphodiester bonds in the folded RNAs in a specific fashion. Imidazole buffer induces cleavages preferentially in single-stranded regions because nucleotides in these regions have more conformational freedom and can assume more easily the geometry needed for formation of the hydrolysis intermediate state. Spermine-imidazole constructs supplemented with free imidazole cleave tRNA(Asp) within single-stranded regions after pyrimidine residues with a marked preference for pyrimidine-A sequences. Hydrolysis patterns suggest a cleavage mechanism involving an attack by the imidazole residue of the electrostatically bound spermine-imidazole and by free imidazole at the most accessible single-stranded regions of the RNA. Cleavages in a viral RNA fragment recapitulating a tRNA-like domain were found in agreement with the model of this molecule that accounts for its functional properties, thus illustrating the potential of the imidazole-derived reagents as structural probes for solution mapping of RNAs. The cleavage reactions are simple to perform, provide information reflecting the state of the ribose-phosphate backbone of RNA and can be used for mapping single- and double-stranded regions in RNAs.},
note = {0305-1048
Journal Article},
keywords = {Asp/*chemistry/genetics/*metabolism RNA, Base Sequence Binding Sites Buffers Hydrolysis Imidazoles Molecular Probes Molecular Sequence Data Molecular Structure Nucleic Acid Conformation RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Tobacco Mosaic Virus/genetics/metabolism, Transfer, Unité ARN, Viral/chemistry/genetics/metabolism Saccharomyces cerevisiae/genetics/metabolism Spermine Support},
pubstate = {published},
tppubtype = {article}
}
Gabryszuk J, Keith G, Monko M, Kuligowska E, Dirheimer G, Szarkowski J W, Przykorska A
Structural specificity of nuclease from wheat chloroplasts stroma Article de journal
Dans: Nucleic Acids Symp Ser, no. 33, p. 115-119, 1995, ISBN: 8643343, (0261-3166 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer, Unité ARN
@article{,
title = {Structural specificity of nuclease from wheat chloroplasts stroma},
author = {J Gabryszuk and G Keith and M Monko and E Kuligowska and G Dirheimer and J W Szarkowski and A Przykorska},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8643343},
isbn = {8643343},
year = {1995},
date = {1995-01-01},
journal = {Nucleic Acids Symp Ser},
number = {33},
pages = {115-119},
abstract = {A single-strand-specific nuclease from wheat chloroplasts (ChS nuclease) was tested as a tool for RNA secondary and tertiary structure investigations, using yeast tRNA(Phe) and yeast tRNA(Asp) as models. In tRNA(Phe) the nuclease introduced main primary cleavages at positions U33, A35 and A36 in the anticodon-loop and G18 and G19 in the D-loop. In tRNA(Asp) the main primary cleavages occurred at positions U33, G34 and U35 in the anticodon-loop and the lower one at position C20:1 in the D-loop. No primary cleavages were observed within the double-stranded stems. Because ChS nuclease has (i) a low molecular weight, (ii) a wide pH range of action (5.0 to 7.5) (iii) no divalent cation requirement in the reaction mixture and (iv) can be obtained as a pure protein in rather large quantities it appeared to be a very good tool for secondary and tertiary structural studies of RNAs.},
note = {0261-3166
Journal Article},
keywords = {Asp/chemistry/genetics/metabolism RNA, Base Sequence Binding Sites Chloroplasts/*enzymology Endonucleases/isolation & purification/*metabolism Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/metabolism RNA, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Triticum/*enzymology, Phe/chemistry/genetics/metabolism Substrate Specificity Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}