Publications
1997
Sissler M, Eriani G, Martin F, Giege R, Florentz C
Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase Article de journal
Dans: Nucleic Acids Res, vol. 25, no. 24, p. 4899-4906, 1997, ISBN: 9396794, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/chemistry Arginine-tRNA Ligase/classification/*metabolism Aspartate-tRNA Ligase/classification/*metabolism Base Sequence DNA Footprinting Escherichia coli Fungal Proteins/classification/*metabolism Models, Arg/chemistry/*metabolism RNA, Asp/chemistry/*metabolism Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/metabolism Stereoisomerism Substrate Specificity Support, ERIANI, FLORENTZ, Fungal/chemistry/*metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation Protein Binding RNA, Non-U.S. Gov't, SISSLER, Transfer, Unité ARN
@article{,
title = {Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase},
author = {M Sissler and G Eriani and F Martin and R Giege and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9396794},
isbn = {9396794},
year = {1997},
date = {1997-01-01},
journal = {Nucleic Acids Res},
volume = {25},
number = {24},
pages = {4899-4906},
abstract = {Gene cloning, overproduction and an efficient purification protocol of yeast arginyl-tRNA synthetase (ArgRS) as well as the interaction patterns of this protein with cognate tRNAArgand non-cognate tRNAAspare described. This work was motivated by the fact that the in vitro transcript of tRNAAspis of dual aminoacylation specificity and is not only aspartylated but also efficiently arginylated. The crystal structure of the complex between class II aspartyl-tRNA synthetase (AspRS) and tRNAAsp, as well as early biochemical data, have shown that tRNAAspis recognized by its variable region side. Here we show by footprinting with enzymatic and chemical probes that transcribed tRNAAspis contacted by class I ArgRS along the opposite D arm side, as is homologous tRNAArg, but with idiosyncratic interaction patterns. Besides protection, footprints also show enhanced accessibility of the tRNAs to the structural probes, indicative of conformational changes in the complexed tRNAs. These different patterns are interpreted in relation to the alternative arginine identity sets found in the anticodon loops of tRNAArgand tRNAAsp. The mirror image alternative interaction patterns of unmodified tRNAAspwith either class I ArgRS or class II AspRS, accounting for the dual identity of this tRNA, are discussed in relation to the class defining features of the synthetases. This study indicates that complex formation between unmodified tRNAAspand either ArgRS and AspRS is solely governed by the proteins.},
note = {0305-1048
Journal Article},
keywords = {Anticodon/chemistry Arginine-tRNA Ligase/classification/*metabolism Aspartate-tRNA Ligase/classification/*metabolism Base Sequence DNA Footprinting Escherichia coli Fungal Proteins/classification/*metabolism Models, Arg/chemistry/*metabolism RNA, Asp/chemistry/*metabolism Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/metabolism Stereoisomerism Substrate Specificity Support, ERIANI, FLORENTZ, Fungal/chemistry/*metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation Protein Binding RNA, Non-U.S. Gov't, SISSLER, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}