Publications
2000
Becker H D, Min B, Jacobi C, Raczniak G, Pelaschier J, Roy H, Klein S, Kern D, Soll D
The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln) Article de journal
Dans: FEBS Lett, vol. 476, no. 3, p. 140-144, 2000, ISBN: 10913601, (0014-5793 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Cloning, Amino Acyl/*metabolism Recombinant Proteins/chemistry/genetics/metabolism Sequence Deletion Substrate Specificity Support, Bacterial Molecular Sequence Data Nitrogenous Group Transferases/chemistry/genetics/*metabolism Protein Structure, Bacterial/metabolism RNA, Molecular Escherichia coli/genetics Genes, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Quaternary RNA, Transfer, Unité ARN
@article{,
title = {The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln)},
author = {H D Becker and B Min and C Jacobi and G Raczniak and J Pelaschier and H Roy and S Klein and D Kern and D Soll},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10913601},
isbn = {10913601},
year = {2000},
date = {2000-01-01},
journal = {FEBS Lett},
volume = {476},
number = {3},
pages = {140-144},
abstract = {Thermus thermophilus strain HB8 is known to have a heterodimeric aspartyl-tRNA(Asn) amidotransferase (Asp-AdT) capable of forming Asn-tRNA(Asn) [Becker, H.D. and Kern, D. (1998) Proc. Natl. Acad. Sci. USA 95, 12832-12837]. Here we show that, like other bacteria, T. thermophilus possesses the canonical set of amidotransferase (AdT) genes (gatA, gatB and gatC). We cloned and sequenced these genes, and constructed an artificial operon for overexpression in Escherichia coli of the thermophilic holoenzyme. The overproduced T. thermophilus AdT can generate Gln-tRNA(Gln) as well as Asn-tRNA(Asn). Thus, the T. thermophilus tRNA-dependent AdT is a dual-specific Asp/Glu-AdT resembling other bacterial AdTs. In addition, we observed that removal of the 44 carboxy-terminal amino acids of the GatA subunit only inhibits the Asp-AdT activity, leaving the Glu-AdT activity of the mutant AdT unaltered; this shows that Asp-AdT and Glu-AdT activities can be mechanistically separated.},
note = {0014-5793
Journal Article},
keywords = {Amino Acid Sequence Cloning, Amino Acyl/*metabolism Recombinant Proteins/chemistry/genetics/metabolism Sequence Deletion Substrate Specificity Support, Bacterial Molecular Sequence Data Nitrogenous Group Transferases/chemistry/genetics/*metabolism Protein Structure, Bacterial/metabolism RNA, Molecular Escherichia coli/genetics Genes, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Quaternary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1993
Poterszman A, Plateau P, Moras D, Blanquet S, Mazauric M H, Kreutzer R, Kern D
Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases Article de journal
Dans: FEBS Lett, vol. 325, no. 3, p. 183-186, 1993, ISBN: 8319804, (0014-5793 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acid Sequence Aspartate-tRNA Ligase/chemistry/*genetics/metabolism Base Sequence Cloning, Bacterial Models, Molecular Crystallization Genes, Molecular Molecular Sequence Data Oligodeoxyribonucleotides Sequence Homology, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Unité ARN
@article{,
title = {Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases},
author = {A Poterszman and P Plateau and D Moras and S Blanquet and M H Mazauric and R Kreutzer and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8319804},
isbn = {8319804},
year = {1993},
date = {1993-01-01},
journal = {FEBS Lett},
volume = {325},
number = {3},
pages = {183-186},
abstract = {The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strain VK-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 A resolution (space group P2(1)2(1)2(1)},
note = {0014-5793
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Aspartate-tRNA Ligase/chemistry/*genetics/metabolism Base Sequence Cloning, Bacterial Models, Molecular Crystallization Genes, Molecular Molecular Sequence Data Oligodeoxyribonucleotides Sequence Homology, Non-U.S. Gov't Thermus thermophilus/*enzymology/genetics, Unité ARN},
pubstate = {published},
tppubtype = {article}
}