Factors determining the specificity of the tRNA aminoacylation reaction

Ebel, Jean‐Pierre; Giegé, Richard; Bonnet, Jacques; Kern, Daniel; Befort, N.; Bollack, C; Fasiolo, Franco; Gangloff, Jean; Dirheimer, G.

doi:10.1016/s0300-9084(73)80415-8

Cited by 188 publications

(99 citation statements)

References 44 publications

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“…Under all these experimental conditions we did not find any significant difference between the K , values measured in cognate or non-cognate systems. This observation is similar to studies with other synthetases [l, 3,26,28,31] and suggests that strong interactions do occur between the wrong tRNAs and the valyl-tRNA synthetase from B. stearothermophilus.…”

Section: Characteristics Of the Misaminoacylation Reactionssupporting

confidence: 89%

“…U pair and tRNAyet from E. coli, the least aminoacylated tRNA species, possesses even a non-paired CA pair a t this position. We propose that this base pair, and more generally the end of the CCA stem is involved in determining the aminoacylation rate of the tRNAs in the presence of valyl-tRNA synthetase [3]. Also the anticodon region of tRNA may be involved in this mechanism.…”

Section: General Conclusionmentioning

confidence: 94%

“…This seems to be a general property of the yeast enzymes, since we found that aspartyl-and phenylalanyltRNA synthetases produce important mischarging [Z, 3,9], whereas the corresponding enzymes from Notewortly is that Cedergren et al [38], from a mathematical analysis of tRNA sequences, came to a similar conclusion namely that tRNAVa1, tRNAMet, tRNAPhe, tRNAIle but also some additional tRNA species such as tRNAAla, tRNATyr and tRNATrp, are more closely related than could be statistically expected and seem to Form a group which has a low mutational distance. I n a similar study, Holmquist et al [41] also concluded that E. coli tRNAVa1 is related with four %on-valine" tRNAs from E. coli which include tRNAMet, tRNAI1e and also tRNAG1y and tRNAArg.…”

Section: General Conclusionmentioning

confidence: 99%

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

et al. 1974

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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. I n 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 tRNAVa1 and noncognate 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 tRNA,Met and of yeast tRNA,Met and tRNAPhe. These reactions are characterized by K , 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. I n the presence of dimethylsulfoxide, the rate and the extent of those misacylation reactions are enhanced. I n the case of E . coli tRNAPhe, the misacylation occurs only in the presence of the organic solvent. I n no case however, new aminoacylation errors are induced a t 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 a t 30 "C has been observed a t higher temperature. Thus organic solvent and heat must have distinct effects on the essential parameters determining the specificity of the tRNA aminoacylation reactions.Also it has been observed that the most easily misacylated tRNA species by valyl-tRNA synthetase from B. stearothermophilus are the same as those which are misacylated by the valyltRNA synthetases from E . coli and from yeast. This observation suggests the existence of a family of tRNAs containing besides of tRNAVB', other tRNAs such as tRNATle, tRNAyet and tRNAPhe, and which are likely to be related from a phylogenic point of view. Moreover these tRNA species have also been found to be easily misacylated by other aminoacyl-tRNA synthetases namely the enzymes specific for isoleucine and phenylalanine, thus suggesting more generally the existence of interacting tRNA-aminoacyl-tRNA synthetase families.The possibility of the tRNAs to be enzymatically mischarged with a wrong amino acid seems to be a rather general feature as numerous incorrect aminoacylation systems have now been described [i -31 (and references therein). These mischarging reactions have especially been detected in vitro, under various experimental conditions, either in heterologous systems where the enzyme and the tRNA came from different sources, but also in homologous systems, where one pure tRNA species interacts Enzyme. Valyl-tRNA synthetase (EC 6.1.1.9). Eur. J. Biochem. 45 (1974)with one non-cognate pure ...

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Section: Characteristics Of the Misaminoacylation Reactionssupporting

confidence: 89%

Section: General Conclusionmentioning

confidence: 94%

Section: General Conclusionmentioning

confidence: 99%

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

et al. 1974

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“…High concentrations of salt generally seem to inhibit the aminoacylation reaction, the only exception known being the esterification of tRNA from halophilic organisms [6]. Extremely high salt concentrations also stimulate the aminoacylation of yeast tRNA phe by the phenylalanyl-tRNA synthetase fromEscherichia coli [7], whereas generally the aminoacylation of non-cognate tRNAs is favored by low ionic strength [8]. Various explanations of the different salt effects were proposed, among them a saltdependent conformational change of the synthetase [4], stabilization of a certain tRNA conformation [2,9], or an interference by salt with the interaction between synthetase and tRNA [1,10].…”

Section: Introductionmentioning

confidence: 99%

The mechanism of salt‐induced stimulation of tRNA^Ser aminoacylation by yeast seryl‐tRNA synthetase

Dibbelt

Zachau

1981

FEBS Letters

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“…A similar observation with tRNAVal and tRNAPh' from yeast has been reported by Ebel et LEI. [2]. Very recently the latter group of authors published a more detailed study on the binding properties of tRNA""' and tRNAPh' from yeast to their cognate synthetases after stepwise removal from these tRNAs of seven nucleotides [3].…”

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confidence: 99%

Thermal Melting Curves of tRNAPhe from Yeast Lacking Different Numbers of Nucleotides from the 3'-End

1976

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The thermal melting curves of tRNAPhe and tRNALys from yeast lacking different numbers of nucleotides from the 3'-end were recorded. The removal of the first nucleotide had no effect on the melting profile. The stepwise removal of the following six nucleotides caused changes in the character of the derivative melting curves : they became rather broad and melting started at lower temperatures. These results indicate that the nucleotides at the 3'-end contribute to the stability of the molecular structure of tRNAs.

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Factors determining the specificity of the tRNA aminoacylation reaction

Cited by 188 publications

References 44 publications

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

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

The mechanism of salt‐induced stimulation of tRNA^Ser aminoacylation by yeast seryl‐tRNA synthetase

Thermal Melting Curves of tRNAPhe from Yeast Lacking Different Numbers of Nucleotides from the 3'-End

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Factors determining the specificity of the tRNA aminoacylation reaction

Cited by 188 publications

References 44 publications

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

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

The mechanism of salt‐induced stimulation of tRNASer aminoacylation by yeast seryl‐tRNA synthetase

Thermal Melting Curves of tRNAPhe from Yeast Lacking Different Numbers of Nucleotides from the 3'-End

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The mechanism of salt‐induced stimulation of tRNA^Ser aminoacylation by yeast seryl‐tRNA synthetase