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• W2017669909 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 tRNAArg and non-cognate tRNAAsp are described. This work was motivated by the fact that the in vitro transcript of tRNAAsp is 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 tRNAAsp is recognized by its variable region side. Here we show by footprinting with enzymatic and chemical probes that transcribed tRNA-Asp is 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 tRNAArg and tRNAAsp. The mirror image alternative interaction patterns of unmodified tRNAAsp with 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 tRNAAsp and either ArgRS and AspRS is solely governed by the proteins." @default.
• W2017669909 created "2016-06-24" @default.
• W2017669909 creator A5001476495 @default.
• W2017669909 date "1997-12-15" @default.
• W2017669909 modified "2023-10-09" @default.
• W2017669909 title "Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase" @default.
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• W2017669909 doi "https://doi.org/10.1093/nar/25.24.4899" @default.
• W2017669909 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/147145" @default.
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