Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase.

Walter, P.; Gangloff, Jean; Bonnet, Jacques; Boulanger, Yves; Ebel, Jean‐Pierre; Fasiolo, Franco

doi:10.1073/pnas.80.9.2437

Cited by 72 publications

(28 citation statements)

References 17 publications

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“…The region of Met-tRNA synthetase located at this position in the model (residues 356-360) forms the sequence Arg-Tyr-Tyr-Tyr-Thr and is thus similarly capable of polar interaction with the tRNA. This sequence is well-conserved in Met-tRNA synthetase enzymes from other organisms (25,26).…”

Section: Resultsmentioning

confidence: 99%

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.

Perona

Rould

Steitz

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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Detailed comparisons between the structures of the tRNA-bound Eschenchia coli glutaminyl-tRNA (GintRNA) synthetase [L-glutamine:tRNAcE ligase (AMP-forming), EC 6.1.1.18] and recently refined E. coli methionyl-tRNA (Met-tRNA) synthetase [L-methionine:tRNAMe ligase (AMPforming), EC 6.1.1.101 reveal icant imilarities beyond the anticipated correspondence of their respective dinudeotide-fold domains. One similarity comprises a 23-amino acid a-helixturn-(,-strand motif found in each enzyme within a domain that is inserted between the two halves of the dinudeotide binding fold. A second correspondence, which consists of two a-helices connected by a large loop and 13-strand, is located in the Gln-tRNA synthetase within a region that binds the inside corner of the "L"-shaped tRNA molecule. This stutural motif contains a long a-helix, which extends along the entire length of the D and anticodon stems of the complexed tRNA. We suggest that the positioning of this helix relative to the dinucleotide fold plays a critical role in ensuring the proper global orientation of tRNAGhn on the surface of the enzyme. The structural correspondences suggest a similar overall orientation of binding of tRNAMel and tRNAGID to their respective synthetases.

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Section: Resultsmentioning

confidence: 99%

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.

Perona

Rould

Steitz

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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“…In this regard it is interesting that for S. cerevisiae and humans the carboxyl-terminal EMAP II-like domain in methionyl-tRNA synthetase has been lost, and its function appears to have been replaced by Arc1p in S. cerevisiae and EMAP II in humans (EMAP II is identical to the p18 component of the 24 S aminoacyl-tRNA synthetase complex), 6 both of which interact with more than one aminoacyl-tRNA synthetase. The selective advantage of allowing multiple aminoacyl-tRNA synthetases to have access to the EMAP II-like domain is reflected in the observation that replacement of the carboxyl-terminal domain by a separate protein occurred at least twice during the evolution of eukaryotic methionyl-tRNA synthetases since this domain is absent in the methionyl-tRNA synthetases from both S. cerevisiae and humans but is present in methionyl-tRNA synthetase from C. elegans (49,60,61).…”

Section: Resultsmentioning

confidence: 99%

Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Kleeman¹,

Wei²,

Simpson

et al. 1997

Journal of Biological Chemistry

116

102

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To test the hypothesis that tRNA Tyr recognition differs between bacterial and human tyrosyl-tRNA synthetases, we sequenced several clones identified as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Project. We found that human tyrosyl-tRNA synthetase is composed of three domains: 1) an aminoterminal Rossmann fold domain that is responsible for formation of the activated E⅐Tyr-AMP intermediate and is conserved among bacteria, archeae, and eukaryotes; 2) a tRNA anticodon recognition domain that has not been conserved between bacteria and eukaryotes; and 3) a carboxyl-terminal domain that is unique to the human tyrosyl-tRNA synthetase and whose primary structure is 49% identical to the putative human cytokine endothelial monocyte-activating protein II, 50% identical to the carboxyl-terminal domain of methionyl-tRNA synthetase from Caenorhabditis elegans, and 43% identical to the carboxyl-terminal domain of Arc1p from Saccharomyces cerevisiae. The first two domains of the human tyrosyl-tRNA synthetase are 52, 36, and 16% identical to tyrosyl-tRNA synthetases from S. cerevisiae, Methanococcus jannaschii, and Bacillus stearothermophilus, respectively. Nine of fifteen amino acids known to be involved in the formation of the tyrosyl-adenylate complex in B. stearothermophilus are conserved across all of the organisms, whereas amino acids involved in the recognition of tRNA Tyr are not conserved. Kinetic analyses of recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed in Escherichia coli indicate that human tyrosyl-tRNA synthetase aminoacylates human but not B. stearothermophilus tRNA Tyr , and vice versa, supporting the original hypothesis. It is proposed that like endothelial monocyte-activating protein II and the carboxyl-terminal domain of Arc1p, the carboxyl-terminal domain of human tyrosyltRNA synthetase evolved from gene duplication of the carboxyl-terminal domain of methionyl-tRNA synthetase and may direct tRNA to the active site of the enzyme.Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. For most aminoacyl-tRNA synthetases (E), tRNA aminoacylation can be separated into two steps: formation of a stable enzyme-bound aminoacyladenylate intermediate (E⅐AA-AMP, Equation 1), followed by transfer of the amino acid (AA) from the aminoacyl-adenylate intermediate to the 3Ј end of the tRNA substrate (Equation 2).The 20 different aminoacyl-tRNA synthetases fall into two distinct structural classes (1, 2). Class I aminoacyl-tRNA synthetases (of which tyrosyl-tRNA synthetase is a member) are characterized by a structurally well conserved amino-terminal Rossmann fold domain which contains the signature sequences "HIGH" and "KMSKS" (3, 4). In contrast, the carboxyl-terminal domains of class I aminoacyl-tRNA synthetases are structurally diverse suggesting that the primordial aminoacyl-tRNA synthetase consisted solely of the amino-terminal Rossmann fold (5-8). Both x-ray crystallography and site-directed mutagenesis of class I aminoacyl-tRNA synthet...

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“…Finally, the two enzymes do not appear to share substantial sequence similarity, at least at the level of their respective gene sequences. This conclusion is based on the fact that we were unable to identify the gene encoding the mt-MetRS by low-stringency DNA-DNA hybridizations using probes of the MESl gene located within the region of highest similarity between the yeast and E. coli enzymes [15]. In contrast, the yeast mitochondrial and cytoplasmic threonyl-tRNA synthetases show a high degree of similarity, so that it was possible to isolate the gene of the cytoplasmic enzyme by using a gene probe of the mitochondrial protein [40].…”

Section: Discussionmentioning

confidence: 99%

Purification of the yeast mitochondrial methionyl‐tRNA synthetase

Schwob

Sanni

Fasiolo

et al. 1988

European Journal of Biochemistry

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Yeast-mitochondria1 methionyl-tRNA synthetase was purified 1060-fold from mitochondrial matrix proteins of Saccharomyces cerevisiae using a four-step procedure based on affinity chromatography (heparin-Ultrogel, tRNAMe'-Sepharose, Agarose-hexyl-AMP) to yield a single polypeptide of high specific activity (1800 U/mg). Like the cytoplasmic methionyl-tRNA synthetase ( M , 85 000), the mitochondrial isoenzyme is a monomer, but of significantly smaller polypeptide size ( M , 65 000). In contrast, the corresponding enzyme of Escherichia coli is a dimer (Mr 152000) made up of identical subunits. The measured affinity constants of the purified mitochondrial enzyme for methionine and tRNA'" are similar to those of the cytoplasmic isoenzyme. However, the two yeast enzymes exhibit clearly different patterns of aminoacylation of heterologous yeast and E. coli tRNAMe'. Furthermore, polyclonal antibodies raised against the two proteins did not show any cross-reactivity by inhibition of enzymatic activity and by the highly sensitive immunoblotting technique, indicating that the two enzymes share little, if any, common antigenic determinants. Taken together, our results further support the belief that the yeast mitochondrial and cytoplasmic methionyl-tRNA synthetases are different proteins coded for by two distinct nuclear genes.Like the yeast cytoplasmic aminoacyl-tRNA synthetases, the mitochondrial enzymes displayed affinity for immobilized heparin. This distinguishes them from the corresponding enzymes of E. coli. Such an unexpected property of the mitochondrial enzymes suggests that they have acquired during evolution a domain for binding to negatively charged cellular components.The components of the yeast mitochondrial translation apparatus are of dual origin. While the mitochondrial (mt) DNA codes for a complete set of transfer RNAs and the 15s and 21s ribosomal RNAs, the proteins required for mitochondrial protein synthesis such as the ribosomal proteins, the aminoacyl-tRNA synthetases, and the translation factors are coded for by nuclear genes. The sole exception is the ribosomal protein varl which is encoded by the mt DNA (for reviews, see [l, 21).Aminoacyl-tRNA synthetases constitute a divergent family of enzymes differing in size and subunit structure but catalyzing the same reaction, the selective attachment of amino acids to their cognate tRNAs. The molecular and catalytic properties of these enzymes have been extensively studied over the past 20 years [3, 41. However, information about mitochondrial aminoacyl-t RNA synthetases remained scarce until recently. Previous studies on phenylalanyl-, leucyl-, and methionyl-tRNA synthetases from yeast mitochondria and cytoplasm indicated that the two isoenzymes exhibit distinctive properties [5 -71. By contrast, no significant differences could be observed between the mitochondrial and cytoplasmic valyl-tRNA synthetases IS]. Recently, cloning and molecular analysis of genes coding for mitochondrial aminoacyl-tRNA synthetases revealed the existence of two classes of nuclea...

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Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase.

Cited by 72 publications

References 17 publications

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.

Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Purification of the yeast mitochondrial methionyl‐tRNA synthetase

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