Publications

• Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase.

  Kim S.I., Soll D.

  Early investigations revealed that Bacillus subtilis glutamyl-tRNA synthetase [GluRS (bs)] is responsible for aminoacylating both glutamate tRNA [tRNA(Glu) (bs)] and glutamine tRNA [tRNA(Gln) (bs)] with glutamate. The same Bacillus enzyme can also efficiently attach glutamate to one isoacceptor gl ... >> More

  Early investigations revealed that Bacillus subtilis glutamyl-tRNA synthetase [GluRS (bs)] is responsible for aminoacylating both glutamate tRNA [tRNA(Glu) (bs)] and glutamine tRNA [tRNA(Gln) (bs)] with glutamate. The same Bacillus enzyme can also efficiently attach glutamate to one isoacceptor glutamine tRNA [tRNA(Gln) (ec)] of Escherichia coli in vitro but not to tRNA2(Gln) (ec) and tRNA(Glu) (ec). To characterize identity elements of these glutamine tRNAs in the interaction with GluRS (bs), tRNA2(Gln) (ec), tRNA1(Gln) (ec), three other mutant glutamine tRNAs [tRNA2(Gln) (AU) (C34 --> U34), tRNA2(Gln) (12M) (C34 --> U34, 31A-U39 --> 31U-A39), and tRNA2(Gln) (M21) (64C --> G50 --> 64G-C50, 63U-A51 --> 63A-U51)] originated from tRNA2(Gln) (ec), tRNA(Gln) (bs), and a mutant tRNAM(Gln) (bs) whose U at the 34th position (U34), was replaced to C (C34), were produced in E. coli. All of the E. coli glutamine tRNAs containing U34 such as tRNA1(Gln), tRNA2(Gln) (AU), and tRNA2(Gln) (12M) could be charged with glutamate by GluRS (bs), whereas tRNA2(Gln) (ec) and its T-stem mutant tRNA2(Gln) (M21) containing C34 could not be charged by the same enzyme. The unique change of C34 to U34 of tRNA2(Gln) (ec) acquired glutamate acceptor activity by GluRS (bs). This result suggests that the U34 is the major identity element of tRNA1(Gln) (ec) in the recognition by GluRS (bs). The same situation was found in tRNA(Gln) (bs). The glutamate acceptor activity of tRNA(Gln) (bs) disappeared on replacement of U34 to C34. To find out whether modified bases in tRNA(Gln) (bs) are involved in the recognition by GluRS (bs), glutamylation of tRNA(Gln) (bs) produced by in vitro transcription was also examined but the in vitro transcript of tRNA(Gln) (bs) could not be charged with glutamic acid by GluRS (bs). All of these mean that the major recognition element for GluRS (bs) is U at the 34th position of both tRNA(Gln) (bs) and tRNA1(Gln) (ec) as a modified form. << Less

  Mol Cells 8:459-465(1998) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Aminoacyl-tRNA synthesis.

  Ibba M., Soll D.

  Aminoacyl-tRNAs are substrates for translation and are pivotal in determining how the genetic code is interpreted as amino acids. The function of aminoacyl-tRNA synthesis is to precisely match amino acids with tRNAs containing the corresponding anticodon. This is primarily achieved by the direct a ... >> More

  Aminoacyl-tRNAs are substrates for translation and are pivotal in determining how the genetic code is interpreted as amino acids. The function of aminoacyl-tRNA synthesis is to precisely match amino acids with tRNAs containing the corresponding anticodon. This is primarily achieved by the direct attachment of an amino acid to the corresponding tRNA by an aminoacyl-tRNA synthetase, although intrinsic proofreading and extrinsic editing are also essential in several cases. Recent studies of aminoacyl-tRNA synthesis, mainly prompted by the advent of whole genome sequencing and the availability of a vast body of structural data, have led to an expanded and more detailed picture of how aminoacyl-tRNAs are synthesized. This article reviews current knowledge of the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis. << Less

  Annu Rev Biochem 69:617-650(2000) [PubMed] [EuropePMC]

  This publication is cited by 26 other entries.

• Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.

  Schmitt E., Moulinier L., Fujiwara S., Imanaka T., Thierry J.-C., Moras D.

  The crystal structure of aspartyl-tRNA synthetase (AspRS) from Pyrococcus kodakaraensis was solved at 1.9 A resolution. The sequence and three-dimensional structure of the catalytic domain are highly homologous to those of eukaryotic AspRSs. In contrast, the N-terminal domain, whose function is to ... >> More

  The crystal structure of aspartyl-tRNA synthetase (AspRS) from Pyrococcus kodakaraensis was solved at 1.9 A resolution. The sequence and three-dimensional structure of the catalytic domain are highly homologous to those of eukaryotic AspRSs. In contrast, the N-terminal domain, whose function is to bind the tRNA anticodon, is more similar to that of eubacterial enzymes. Its structure explains the unique property of archaeal AspRSs of accommodating both tRNAAsp and tRNAAsn. Soaking the apo-enzyme crystals with ATP and aspartic acid both separately and together allows the adenylate formation to be followed. Due to the asymmetry of the dimeric enzyme in the crystalline state, different steps of the reaction could be visualized within the same crystal. Four different states of the aspartic acid activation reaction could thus be characterized, revealing the functional correlation of the observed conformational changes. The binding of the amino acid substrate induces movement of two invariant loops which secure the position of the peptidyl moiety for adenylate formation. An unambiguous spatial and functional assignment of three magnesium ion cofactors can be made. This study shows the important role of residues present in both archaeal and eukaryotic AspRSs, but absent from the eubacterial enzymes. << Less

  EMBO J. 17:5227-5237(1998) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.