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Incorrect Aminoacylations Involving tRNAs or Valyl-tRNA Synthetase from BacilIus stearothermophilus

1974; Wiley; Volume: 45; Issue: 2 Linguagem: Inglês

10.1111/j.1432-1033.1974.tb03560.x

ISSN

1432-1033

Autores

Richard Giegé, Daniel Kern, Jean‐Pierre Ebel, S. de Henau, Hubert Chantrenne, Henri Grosjean,

Tópico(s)

Mass Spectrometry Techniques and Applications

Resumo

European Journal of BiochemistryVolume 45, Issue 2 p. 351-362 Free Access Incorrect Aminoacylations Involving tRNAs or Valyl-tRNA Synthetase from BacilIus stearothermophilus Richard Giegé, Richard Giegé Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, U.S.A. 02139Search for more papers by this authorDaniel Kern, Daniel Kern Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., 15 Rue Descartes, F-67000 Strasbourg, FranceSearch for more papers by this authorJean-Pierre Ebel, Jean-Pierre Ebel Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., 15 Rue Descartes, F-67000 Strasbourg, FranceSearch for more papers by this authorSuzanne De henau, Suzanne De henau Laboratoire de Chiniie Biologique, Faculté des Sciences de I'U.L.B., 67 Rue des Chevaux, B-1640 Rhode-St-Genhse, BelgiumSearch for more papers by this authorHubert Chantrenne, Hubert Chantrenne Laboratoire de Chiniie Biologique, Faculté des Sciences de I'U.L.B., 67 Rue des Chevaux, B-1640 Rhode-St-Genhse, BelgiumSearch for more papers by this authorHenri Grosjean, Henri Grosjean Department of Molecular Biophysics and Biochemistry, Yale University, Box 1937, Yale Station, New Haven, Connecticut, U.S.A. 06520Search for more papers by this author Richard Giegé, Richard Giegé Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, U.S.A. 02139Search for more papers by this authorDaniel Kern, Daniel Kern Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., 15 Rue Descartes, F-67000 Strasbourg, FranceSearch for more papers by this authorJean-Pierre Ebel, Jean-Pierre Ebel Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., 15 Rue Descartes, F-67000 Strasbourg, FranceSearch for more papers by this authorSuzanne De henau, Suzanne De henau Laboratoire de Chiniie Biologique, Faculté des Sciences de I'U.L.B., 67 Rue des Chevaux, B-1640 Rhode-St-Genhse, BelgiumSearch for more papers by this authorHubert Chantrenne, Hubert Chantrenne Laboratoire de Chiniie Biologique, Faculté des Sciences de I'U.L.B., 67 Rue des Chevaux, B-1640 Rhode-St-Genhse, BelgiumSearch for more papers by this authorHenri Grosjean, Henri Grosjean Department of Molecular Biophysics and Biochemistry, Yale University, Box 1937, Yale Station, New Haven, Connecticut, U.S.A. 06520Search for more papers by this author First published: June 1974 https://doi.org/10.1111/j.1432-1033.1974.tb03560.xCitations: 81 AboutSectionsPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Numerous misacylations occur on heterologous systems containing unfractionated tRNAs from yeast or from Bacillus stearothermophilus and pure valyl-tRNA synthetase from B. stearothermophilus or from yeast, when special aminoacylation conditions are used. In the homologous system and in heterologous systems where the unfractionated tRNAs and the enzyme originate from prokaryotic organisms (B. stearothermophilus and Escherichia coli), the errors are seldom. This phenomenon is explained by competition effects between the cognate tRNAVal and non-cognate tRNAs for the valyl-tRNA synthetase. But using pure tRNA species, errors can be observed in such systems, even under classical assay conditions; in particular it was shown that the valyl-tRNA synthetase from B. stearothermophilus catalyses the misacylation of E. coli tRNAIle and tRNAtMet and of yeast tRNAtMet and tRNAPhe. These reactions are characterized by Km values slightly increased as compared to the value obtained in the cognate system and by V values decreased by a factor of about 40 to 3000 compared to the cognate tRNA species. In the presence of dimethylsulfoxide, the rate and the extent of those misacylation reactions are enhanced. In the case of E. coli tRNAPhe, the misacylation occurs only in the presence of the organic solvent. In no case however, new aminoacylation errors are induced at high temperature (50–75 °C) in the presence of the thermostable valyl-tRNA synthetase from B. stearothermophilus; only an increase of the rates of the aminoacylation reactions which already occur at 30 °C has been observed at higher temperature. Thus organic solvent and heat must have distinct effects on the essential parameters determining the specificity of the tRNA aminoacylation reactions. 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