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}
}