glutamate trna ligase

Summary

Summary: An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.

Top Publications

  1. Sheppard K, Soll D. On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. J Mol Biol. 2008;377:831-44 pubmed publisher
    ..Archaeal GatCAB, on the other hand, has not favored a distinct tRNA(Asn), suggesting that tRNA(Asn) recognition is not a major barrier to the retention of asparaginyl-tRNA synthetase in many Archaea. ..
  2. Lamour V, Quevillon S, Diriong S, N Guyen V, Lipinski M, Mirande M. Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994;91:8670-4 pubmed
    ..A molecular phylogenetic analysis was conducted on the 14 GlxRS (GluRS or GlnRS) sequences available to date. Our data suggest that bacterial GlnRS has a eukaryotic origin and was acquired by a mechanism of horizontal gene transfer. ..
  3. Frechin M, Senger B, Brayé M, Kern D, Martin R, Becker H. Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev. 2009;23:1119-30 pubmed publisher
    ..This novel strategy that enables a single protein to be localized in both the cytosol and mitochondria provides a new paradigm for regulation of the dynamic subcellular distribution of proteins between membrane-separated compartments. ..
  4. Galani K, Hurt E, Simos G. The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism. FEBS Lett. 2005;579:969-75 pubmed
    ..Thus, the cytoplasmic location of Arc1p is maintained by Xpo1p-dependent nuclear export and Arc1p could act as an adapter in the nucleocytoplasmic trafficking of tRNA and/or the tRNA-aminoacylation machinery. ..
  5. Lee J, Hendrickson T. Divergent anticodon recognition in contrasting glutamyl-tRNA synthetases. J Mol Biol. 2004;344:1167-74 pubmed
    ..As GluRS1 and GluRS2 are related by an apparent gene duplication event, these results demonstrate that we can experimentally map critical evolutionary events in the emergence of new tRNA specificities. ..
  6. Deinert K, Fasiolo F, Hurt E, Simos G. Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem. 2001;276:6000-8 pubmed
  7. Sekine S, Nureki O, Shimada A, Vassylyev D, Yokoyama S. Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Nat Struct Biol. 2001;8:203-6 pubmed publisher
    ..The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'...
  8. Siatecka M, Rozek M, Barciszewski J, Mirande M. Modular evolution of the Glx-tRNA synthetase family--rooting of the evolutionary tree between the bacteria and archaea/eukarya branches. Eur J Biochem. 1998;256:80-7 pubmed
    ..The transient capture of UAA and UAG codons could have favored the emergence of a GlnRS in early eukaryotes. ..
  9. Galani K, Grosshans H, Deinert K, Hurt E, Simos G. The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p. EMBO J. 2001;20:6889-98 pubmed
    ..We suggest that the organization of aminoacyl-tRNA synthetases into a multimeric complex not only affects catalysis, but is also a means of segregating the tRNA- aminoacylation machinery mainly to the cytoplasmic compartment. ..

More Information

Publications62

  1. Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, et al. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 1996;15:5437-48 pubmed
    ..Arc1p is, therefore, a yeast protein with dual specificity: it associates with tRNA and aminoacyl-tRNA synthetases. This functional interaction may be required for efficient aminoacylation in vivo. ..
  2. Paravisi S, Fumagalli G, Riva M, Morandi P, Morosi R, Konarev P, et al. Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution. FEBS J. 2009;276:1398-417 pubmed publisher
    ..tuberculosis proteins can form a complex, which may control the flux of Glu-tRNA(Glu) toward protein or tetrapyrrole biosynthesis...
  3. Schmitt E, Panvert M, Blanquet S, Mechulam Y. Structural basis for tRNA-dependent amidotransferase function. Structure. 2005;13:1421-33 pubmed publisher
    ..Comparison of GatD and L-asparaginase structures shows how the motion of a beta hairpin region containing a crucial catalytic threonine may control the overall reaction cycle of GatDE...
  4. Dubois D, Blais S, Huot J, Lapointe J. A C-truncated glutamyl-tRNA synthetase specific for tRNA(Glu) is stimulated by its free complementary distal domain: mechanistic and evolutionary implications. Biochemistry. 2009;48:6012-21 pubmed publisher
    ..These results confirm the modular nature of GluRS and support the model of a "recent" fusion of domains 4 and 5 to a proto-GluRS containing the catalytic domain and able to recognize its tRNA substrate(s). ..
  5. Santoro S, Anderson J, Lakshman V, Schultz P. An archaebacteria-derived glutamyl-tRNA synthetase and tRNA pair for unnatural amino acid mutagenesis of proteins in Escherichia coli. Nucleic Acids Res. 2003;31:6700-9 pubmed
    ..coli. Development of the glutamic acid orthogonal pair increases the potential diversity of unnatural amino acid structures that may be incorporated into proteins in E.coli. ..
  6. Brown J, Doolittle W. Gene descent, duplication, and horizontal transfer in the evolution of glutamyl- and glutaminyl-tRNA synthetases. J Mol Evol. 1999;49:485-95 pubmed
    ..Although all bacterial GlnRS form a monophyletic group, the broad phyletic distribution of this tRNA synthetase suggests that multiple gene transfers from eukaryotes to bacteria occurred shortly after the Archaea-eukaryote divergence. ..
  7. Blaise M, Becker H, Keith G, Cambillau C, Lapointe J, Giege R, et al. A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon. Nucleic Acids Res. 2004;32:2768-75 pubmed
  8. Perona J. Two-step pathway to aminoacylated tRNA. Structure. 2005;13:1397-8 pubmed
  9. Lefevre T, Arseneault K, Pézolet M. Study of protein aggregation using two-dimensional correlation infrared spectroscopy and spectral simulations. Biopolymers. 2004;73:705-15 pubmed
    ..Thus, one has to be aware that true asynchronisms are not necessarily at the origin of peaks observed in asynchronous maps. ..
  10. Ryu Y, Schultz P. Efficient incorporation of unnatural amino acids into proteins in Escherichia coli. Nat Methods. 2006;3:263-5 pubmed
    ..jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expressed under control of a mutant glnS (glnS') promoter. ..
  11. Simader H, Hothorn M, Köhler C, Basquin J, Simos G, Suck D. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Nucleic Acids Res. 2006;34:3968-79 pubmed
    ..The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors. ..
  12. Gustilo E, Dubois D, Lapointe J, Agris P. E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix. RNA Biol. 2007;4:85-92 pubmed
    ..Thus, the RNA constructs are effective tools to study RNA-protein interaction. ..
  13. Hong K, Ibba M, Weygand Durasevic I, Rogers M, Thomann H, Soll D. Transfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase. EMBO J. 1996;15:1983-91 pubmed
    ..The observed role of RNA as a cofactor in optimizing amino acid activation suggests that the tRNAGln-GlnRS complex may be partly analogous to ribonucleoprotein enzymes where protein-RNA interactions facilitate catalysis. ..
  14. Levican G, Katz A, Valenzuela P, Soll D, Orellana O. A tRNA(Glu) that uncouples protein and tetrapyrrole biosynthesis. FEBS Lett. 2005;579:6383-7 pubmed
    ..Therefore, aminoacylation of tRNA(3)(Glu) might contribute to ensure protein synthesis upon high heme demand by an uncoupling of protein and heme biosynthesis. ..
  15. Campanacci V, Dubois D, Becker H, Kern D, Spinelli S, Valencia C, et al. The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity. J Mol Biol. 2004;337:273-83 pubmed
    ..coli tRNAGlu, but to another, as yet unknown tRNA. These results suggest thus a novel function, distinct from that of GluRSs, for the yadB gene family. ..
  16. Kunze N, Bittler E, Fett R, Schray B, Hameister H, Wiedorn K, et al. The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42. Hum Genet. 1990;85:527-30 pubmed
    ..There are now nine mapped aminoacyl-tRNA synthetase genes in the human genome. ..
  17. Brown S. Time of action of 4.5 S RNA in Escherichia coli translation. J Mol Biol. 1989;209:79-90 pubmed
    ..5 S RNA stabilizes the post-translocation state by replacing 23 S ribosomal RNA as a binding site for elongation factor G. The 4.5 S RNA-requirement of mutants altered in 23 S ribosomal RNA support this model. ..
  18. Gendron N, Breton R, Champagne N, Lapointe J. Adenylosuccinate lyase of Bacillus subtilis regulates the activity of the glutamyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1992;89:5389-92 pubmed
    ..The interaction between these enzymes may play a role in the coordination of purine metabolism and protein biosynthesis. ..
  19. Katz A, Banerjee R, de Armas M, Ibba M, Orellana O. Redox status affects the catalytic activity of glutamyl-tRNA synthetase. Biochem Biophys Res Commun. 2010;398:51-5 pubmed publisher
    ..The sensitivity to oxidation of A. ferrooxidans GluRS1 might provide a means to regulate tetrapyrrole and protein biosynthesis in response to extreme changes in both the redox and heme status of the cell via a single enzyme. ..
  20. Sherman J, Rogers M, Soll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Res. 1992;20:2847-52 pubmed
    ..In addition, we show that the discriminator base (position 73) and the first base of the anticodon are important for recognition by E. coli tyrosyl-tRNA synthetase. ..
  21. Akochy P, Bernard D, Roy P, Lapointe J. Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1. J Bacteriol. 2004;186:767-76 pubmed
    ..Such novel antibiotics could be active against other multidrug-resistant gram-negative pathogens such as Burkholderia and Neisseria as well as all pathogenic gram-positive bacteria. ..
  22. Chang K, Hendrickson T. Recognition of tRNAGln by Helicobacter pylori GluRS2--a tRNAGln-specific glutamyl-tRNA synthetase. Nucleic Acids Res. 2009;37:6942-9 pubmed publisher
    ..Here, we show that GluRS2 recognizes major identity elements clustered in the tRNA(Gln) acceptor stem. Mutations in the tRNA anticodon or at the discriminator base had little to no impact on enzyme specificity and activity. ..
  23. Gungor O, Özkaya A, Sahin Y, Gungor G, Dilber C, Aydin K. A compound heterozygous EARS2 mutation associated with mild leukoencephalopathy with thalamus and brainstem involvement and high lactate (LTBL). Brain Dev. 2016;38:857-61 pubmed publisher
    ..High-throughput sequencing revealed a novel compound heterozygous mutation in mitochondrial glutamyl-tRNA synthetase 2 (EARS2), which appears to be causative of disease symptoms. ..
  24. Arnez J, Steitz T. Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure. Biochemistry. 1994;33:7560-7 pubmed
    ..An identical water-bridging structure is possible at four of the five other psuedo-uridines in known tRNA structures. ..
  25. Frechin M, Duchene A, Becker H. Translating organellar glutamine codons: a case by case scenario?. RNA Biol. 2009;6:31-4 pubmed
    ..Indeed, QRS activity was found in protozoan mitochondria while AdT activity was characterized in plant organelles. The pathway for Q-tRNA(Q) synthesis in yeast and mammals mitochondria is still questionable. ..
  26. Chang C, Chang C, Chakraborty S, Wang S, Tseng Y, Wang C. Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation. J Biol Chem. 2016;291:17102-11 pubmed publisher
  27. Thommes P, Fett R, Schray B, Kunze N, Knippers R. The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988;16:5391-406 pubmed
    ..coli and two times larger than the yeast Gln-tRNA synthetase. The three enzymes share an evolutionarily conserved core but differ in amino acid sequences linked to the N-terminal and C-terminal side of the core. ..
  28. Golinelli Cohen M, Mirande M. Arc1p is required for cytoplasmic confinement of synthetases and tRNA. Mol Cell Biochem. 2007;300:47-59 pubmed
    ..Our results are consistent with a model according to which Arc1p is a bifunctional protein involved in the subcellular localization of ScMetRS and ScGluRS via its N-terminal domain and of tRNA via its C-terminal domain. ..
  29. Banerjee R, Dubois D, Gauthier J, Lin S, Roy S, Lapointe J. The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm. Eur J Biochem. 2004;271:724-33 pubmed
  30. Champagne N, Lapointe J. Influence of FIS on the transcription from closely spaced and non-overlapping divergent promoters for an aminoacyl-tRNA synthetase gene (gltX) and a tRNA operon (valU) in Escherichia coli. Mol Microbiol. 1998;27:1141-56 pubmed
  31. Hu R, Zhao Z, Li L, Li Z, Tang X, Duan L, et al. [Prokaryotic expression and immunization of glutamyl tRNA synthetase of Streptococcus suis]. Wei Sheng Wu Xue Bao. 2010;50:418-22 pubmed
    ..These results proved that GtS has certain immunogenicity and can offer partial protection against high dose challenge. Therefore Gts could be a potential candidate of subunit vaccine against Streptococcus suis. ..
  32. Day I, Golovkin M, Reddy A. Cloning of the cDNA for glutamyl-tRNA synthetase from Arabidopsis thaliana. Biochim Biophys Acta. 1998;1399:219-24 pubmed
    ..Expression of the GluRSAt in E. coli resulted in a protein of the expected size. Comparison of the amino acid sequence GluRSAt to other glutamyl-tRNA synthetases showed strong sequence similarity to cytoplasmic GluRS proteins. ..
  33. Dasgupta S, Saha R, Dey C, Banerjee R, Roy S, Basu G. The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination. FEBS Lett. 2009;583:2114-20 pubmed publisher
    ..coli tRNA(Gln). Our results demonstrate that in addition to the anticodon-binding domain, tRNA(Gln) discriminatory elements may be present in the catalytic domain in E. coli GluRS as well. ..
  34. Cerini C, Semeriva M, Gratecos D. Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex. Eur J Biochem. 1997;244:176-85 pubmed
    ..Overexpression of the repeated motifs leads to a sterility of the flies that suggests a role of these motifs in linking the multienzyme complex to an, as yet, unknown structure of the protein synthesis apparatus. ..
  35. Frechin M, Kern D, Martin R, Becker H, Senger B. Arc1p: anchoring, routing, coordinating. FEBS Lett. 2010;584:427-33 pubmed publisher
  36. Pham V, Maaroufi H, Balg C, Blais S, Messier N, Roy P, et al. Inhibition of Helicobacter pylori Glu-tRNAGln amidotransferase by novel analogues of the putative transamidation intermediate. FEBS Lett. 2016;590:3335-3345 pubmed publisher
    ..The properties of these inhibitors indicate that the 3'-terminal adenine of Glu-tRNAGln plays a major role in binding to the AdT transamidation active site. ..
  37. Englisch Peters S, Conley J, Plumbridge J, Leptak C, Soll D, Rogers M. Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNA(Gln) interaction. Biochimie. 1991;73:1501-8 pubmed
    ..This correlates with the classification of GlnRS as a class I aminoacyl-tRNA synthetase. Mutations in tRNA(Gln) are discussed which affect the recognition of GlnRS and the current concept of glutamine identity in E coli is reviewed. ..
  38. Laberge S, Gagnon Y, Bordeleau L, Lapointe J. Cloning and sequencing of the gltX gene, encoding the glutamyl-tRNA synthetase of Rhizobium meliloti A2. J Bacteriol. 1989;171:3926-32 pubmed
    ..These results suggest that the C-terminal part of the protein is probably not involved in the recognition of substrates, a feature shared with other aminoacyl-tRNA synthetases. ..
  39. Kim Y, Lee J, Cho H, Lee S, Ha H, Kim S, et al. Inactivation of organellar glutamyl- and seryl-tRNA synthetases leads to developmental arrest of chloroplasts and mitochondria in higher plants. J Biol Chem. 2005;280:37098-106 pubmed
    ..This is the first report to analyze the effect of ARS disruption on organelle development in plants. ..
  40. Golinelli Cohen M, Zakrzewska A, Mirande M. Complementation of yeast Arc1p by the p43 component of the human multisynthetase complex does not require its association with yeast MetRS and GluRS. J Mol Biol. 2004;340:15-27 pubmed
    ..We propose that p43/Arc1p may be involved in sequestering tRNAs in the cytoplasm of eukaryotic cells, thereby increasing their availability for protein synthesis. ..
  41. Sekine S, Shichiri M, Bernier S, Ch nevert R, Lapointe J, Yokoyama S. Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Structure. 2006;14:1791-9 pubmed publisher
    ..These structures, together with our previously described structures, reveal that tRNA plays a crucial role in accurate positioning of both L-glutamate and ATP, thus driving the amino acid activation...
  42. Ito T, Kiyasu N, Matsunaga R, Takahashi S, Yokoyama S. Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima. Acta Crystallogr D Biol Crystallogr. 2010;66:813-20 pubmed publisher
    ..Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNA(Gln)...
  43. Black Pyrkosz A, Eargle J, Sethi A, Luthey Schulten Z. Exit strategies for charged tRNA from GluRS. J Mol Biol. 2010;397:1350-71 pubmed publisher
    ..Addition of elongation factor Tu to the aaRS.tRNA complex stimulates the dissociation of the tRNA core and the tRNA acceptor stem. ..
  44. Liu D, Magliery T, Pastrnak M, Schultz P. Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo. Proc Natl Acad Sci U S A. 1997;94:10092-7 pubmed
    ..The mutant GlnRS and engineered tRNA also constitute a functional synthetase-tRNA pair in vivo. The nature of the GlnRS mutations, which occur both at the protein-tRNA interface and at sites further away, is discussed. ..
  45. Núñez H, Lefimil C, Min B, Soll D, Orellana O. In vivo formation of glutamyl-tRNA(Gln) in Escherichia coli by heterologous glutamyl-tRNA synthetases. FEBS Lett. 2004;557:133-5 pubmed
    ..We demonstrate that while Acidithiobacillus ferrooxidans GluRS1 and Bacillus subtilis Q373R GluRS form Glu-tRNA(Glu), A. ferrooxidans and Helicobacter pylori GluRS2 form Glu-tRNA(Gln) in E. coli in vivo. ..
  46. Blaise M, Becker H, Lapointe J, Cambillau C, Giege R, Kern D. Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon. Biochimie. 2005;87:847-61 pubmed
    ..The evolutionary significance of the existence of an aminoacyl-tRNA synthetase paralog dedicated to the hypermodification of a tRNA anticodon will be discussed. ..
  47. Graindorge J, Senger B, Tritch D, Simos G, Fasiolo F. Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity. Biochemistry. 2005;44:1344-52 pubmed
    ..Transcripts of yeast tRNA(Glu) were poor substrates for measuring tRNA aminoacylation and could not be used to clarify whether Arc1p has a specific effect on the tRNA charging reaction. ..
  48. Rogers M, Soll D. Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA. Proc Natl Acad Sci U S A. 1988;85:6627-31 pubmed
    ..This implies that misaminoacylation in vivo is dependent on the competition by different synthetases for the tRNA. In addition, the "translational efficiency" of tRNA is an integral part in observing misaminoacylation in vivo. ..
  49. Luque I, Andújar A, Jia L, Zabulon G, de Marsac N, Flores E, et al. Regulated expression of glutamyl-tRNA synthetase is directed by a mobile genetic element in the cyanobacterium Tolypothrix sp. PCC 7601. Mol Microbiol. 2006;60:1276-88 pubmed
    ..PCC 7601. ISTosp1 constitutes a good example of how cells can make use of a transposable element to evolve an original regulatory mechanism. ..
  50. Liu W, Fu Y, Hu G, Si H, Zhu L, Wu C, et al. Identification and fine mapping of a thermo-sensitive chlorophyll deficient mutant in rice (Oryza sativa L.). Planta. 2007;226:785-95 pubmed
    ..So the OsGluRS gene (TIGR locus Os02 g02860) which encode glutamyl-tRNA synthetase was identified as the Cde1(t) gene. ..
  51. Sahin S, Cansu A, Kalay E, Dinçer T, Kul S, Çakır İ, et al. Leukoencephalopathy with thalamus and brainstem involvement and high lactate caused by novel mutations in the EARS2 gene in two siblings. J Neurol Sci. 2016;365:54-8 pubmed publisher
    ..MRI findings were specific to LTBL. MRI lesions of the older sibling had regressed over time. Clinical and radiological improvement, as in the previously reported patients with LTBL, may be an important clue for diagnosis. ..
  52. Nureki O, Suzuki K, Hara Yokoyama M, Kohno T, Matsuzawa H, Ohta T, et al. Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein. Eur J Biochem. 1992;204:465-72 pubmed
    ..The crystals diffract X-rays beyond 0.35 nm. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters of a = 8.64 nm, b = 8.86 nm and c = 8.49 nm. ..
  53. Faxén M, Plumbridge J, Isaksson L. Codon choice and potential complementarity between mRNA downstream of the initiation codon and bases 1471-1480 in 16S ribosomal RNA affects expression of glnS. Nucleic Acids Res. 1991;19:5247-51 pubmed
    ..We also give evidence that supports the idea that the presence of rare codons near the beginning of the mRNA can affect expression. ..