Purification, Characterization and Mechanism of Action of Several Aminoacyl-tRNA Synthetases from Bacillus Stearothermophilus

Grosjean, Henri; Charlier, Josée; Darte, Claude; Dirheimer, G.; Giegé, Richard; Henau, Suzanne De; Keith, Gérard; Parfait, R.; Takada, C

doi:10.1007/978-3-0348-7675-9_28

Cited by 12 publications

(3 citation statements)

References 21 publications

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“…Related to this view, notice that GluRS from Bacillus stearothermophilus, another close relative of YadB, is able to glutamylate several non-cognate tRNAs. 41 Among the tRNA species that are the most easily glutamylated one finds E. coli tRNA Glu and noncognate initiator tRNA Metf and tRNA Leu2 as well as yeast initiator tRNA Met and tRNA Asp . It is likely that the E. coli tRNA species recognized by YadB share(s) sequence resemblance with the amino acid acceptor stem of the above-listed non-cognate tRNAs.…”

Section: Discussionmentioning

confidence: 99%

The Escherichia coli YadB Gene Product Reveals a Novel Aminoacyl-tRNA Synthetase Like Activity

Campanacci

Dubois

Becker

et al. 2004

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

The Escherichia coli YadB Gene Product Reveals a Novel Aminoacyl-tRNA Synthetase Like Activity

Campanacci

Dubois

Becker

et al. 2004

Journal of Molecular Biology

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“…Finally the discriminator base and the central nucleotide of the anticodon have been found to be arginine identity elements in Escherichia coli tRNA r (McClain et al, 1990;Tamura et al, 1992) and it is likely that a functional relationship exists between prokaryotes and lower eukaryotes. since a prokaryotic ArgRS (from Bacillus steacrothe-niophilius) has been found to charge easily yeast tRNA (Grosjean et al, 1976). The discriminator base is either G or C in yeast tRNAArg isoacceptors and G in tRNAASP.…”

Section: Arginylation Properties Of Selected Trnaasp Variantsmentioning

confidence: 99%

Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts.

1996

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Colresponding authorYeast arginyl-tRNA synthetase recognizes the nonmodified wild-type transcripts derived from both yeast tRNAArg and tRNAASP with equal efficiency. It discriminates its cognate natural substrate, tRNA , from non-cognate tRNAASP by a negative discrimination mechanism whereby a single methyl group acts as an anti-determinant. Considering these facts, recognition elements responsible for specific arginylation in yeast have been searched by studying the in vitro arginylation properties of a series of transcripts derived from yeast tRNAASP, considered as an arginine isoacceptor tRNA. In parallel, experiments on similar tRNAArg transcripts were performed. Unexpectedly, in the tRNAArg context, arginylation is basically linked to the presence of residue C35, whereas in the tRNAASP context, it is deeply related to that of C36 and G37 but is insensitive to the nucleotide at position 35. Each of these nucleotides present in one host, is absent in the other host tRNA. Thus, arginine identity is dependent on two different specific recognition sets according to the tRNA framework investigated.

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“…This possibility is suggested by the fact that certain canonical tRNAs, in particular valine-specific tRNAs, are well known to be mischarged by different aminoacyl-tRNA synthetases (e.g. [22][23][24][25]. Mischarging of viral RNAs might also be expected due to the lack of modified bases, whose absence in tRNA transcripts causes a structural relaxation (26), that results in relaxed specificity: e.g.…”

Section: Introductionmentioning

confidence: 99%

Efficient mischarging of a viral tRNA-like structure and aminoacylation of a minihelix containing a pseudoknot: histidinylation of turnip yellow mosaic virus RNA

Rudinger

Florentz²,

Dreher

et al. 1992

Nucl Acids Res

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Mischarging of the valine specific tRNA-like structure of turnip yellow mosaic virus (TYMV) RNA has been tested in the presence of purified arginyl-, aspartyl-, histidinyl-, and phenylalanyl-tRNA synthetases from bakers' yeast. Important mischarging of a 264 nucleotide-long transcript was found with histidinyl-tRNA synthetase which can acylate this fragment up to a level of 25% with a loss of specificity (expressed as Vmax/KM ratios) of only 100 fold as compared to a yeast tRNA(His) transcript. Experiments on transcripts of various lengths indicate that the minimal valylatable fragment (n = 88) is the most efficient substrate for histidinyl-tRNA synthetase, with kinetic characteristics similar to those found for the control tRNA(His) transcript. Mutations in the anticodon or adjacent to the 3' CCA that severely affect the valylation capacity of the 264 nucleotide long TYMV fragment are without negative effect on its mischarging, and for some cases even improve its efficiency. A short fragment (n = 42) of the viral RNA containing the pseudoknot and corresponding to the amino acid accepting branch of the molecule is an efficient histidine acceptor.

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Purification, Characterization and Mechanism of Action of Several Aminoacyl-tRNA Synthetases from Bacillus Stearothermophilus

Cited by 12 publications

References 21 publications

The Escherichia coli YadB Gene Product Reveals a Novel Aminoacyl-tRNA Synthetase Like Activity

The Escherichia coli YadB Gene Product Reveals a Novel Aminoacyl-tRNA Synthetase Like Activity

Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts.

Efficient mischarging of a viral tRNA-like structure and aminoacylation of a minihelix containing a pseudoknot: histidinylation of turnip yellow mosaic virus RNA

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