HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 275, Issue 42, 32535-32542, October 20, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/42/32535    most recent M005166200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Soutourina, J. Articles by Blanquet, S. Search for Related Content PubMed PubMed Citation Articles by Soutourina, J. Articles by Blanquet, S. Social Bookmarking                      What's this?

Metabolism of D-Aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae Cells^*

Julie Soutourina, Pierre Plateau, and Sylvain Blanquet

From the Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, 91128 Palaiseau Cedex, France

In Escherichia coli, tyrosyl-tRNA synthetase is known to esterify tRNA^Tyr with tyrosine. Resulting D-Tyr-tRNA^Tyr can be hydrolyzed by a D-Tyr-tRNA^Tyr deacylase. By monitoring E. coli growth in liquid medium, we systematically searched for other D-amino acids, the toxicity of which might be exacerbated by the inactivation of the gene encoding D-Tyr-tRNA^Tyr deacylase. In addition to the already documented case of D-tyrosine, positive responses were obtained with D-tryptophan, D-aspartate, D-serine, and D-glutamine. In agreement with this observation, production of D-Asp-tRNA^Asp and D-Trp-tRNA^Trp by aspartyl-tRNA synthetase and tryptophanyl-tRNA synthetase, respectively, was established in vitro. Furthermore, the two D-aminoacylated tRNAs behaved as substrates of purified E. coli D-Tyr-tRNA^Tyr deacylase. These results indicate that an unexpected high number of D-amino acids can impair the bacterium growth through the accumulation of D-aminoacyl-tRNA molecules and that D-Tyr-tRNA^Tyr deacylase has a specificity broad enough to recycle any of these molecules. The same strategy of screening was applied using Saccharomyces cerevisiae, the tyrosyl-tRNA synthetase of which also produces D-Tyr-tRNA^Tyr, and which, like E. coli, possesses a D-Tyr-tRNA^Tyr deacylase activity. In this case, inhibition of growth by the various 19 D-amino acids was followed on solid medium. Two isogenic strains containing or not the deacylase were compared. Toxic effects of D-tyrosine and D-leucine were reinforced upon deprivation of the deacylase. This observation suggests that, in yeast, at least two D-amino acids succeed in being transferred onto tRNAs and that, like in E. coli, the resulting two D-aminoacyl-tRNAs are substrates of a same D-aminoacyl-tRNA deacylase.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Y. Goto, H. Murakami, and H. Suga Initiating translation with D-amino acids RNA, July 1, 2008; 14(7): 1390 - 1398. [Abstract] [Full Text] [PDF]

				A. Sheoran, G. Sharma, and E. A. First Activation of D-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase: 1. PRE-STEADY-STATE KINETIC ANALYSIS REVEALS THE MECHANISTIC BASIS FOR THE RECOGNITION OF D-TYROSINE J. Biol. Chem., May 9, 2008; 283(19): 12960 - 12970. [Abstract] [Full Text] [PDF]

				D. Thompson, C. Lazennec, P. Plateau, and T. Simonson Ammonium Scanning in an Enzyme Active Site: THE CHIRAL SPECIFICITY OF ASPARTYL-tRNA SYNTHETASE J. Biol. Chem., October 19, 2007; 282(42): 30856 - 30868. [Abstract] [Full Text] [PDF]

				S. Wydau, M.-L. Ferri-Fioni, S. Blanquet, and P. Plateau GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase Nucleic Acids Res., February 16, 2007; 35(3): 930 - 938. [Abstract] [Full Text] [PDF]

				M.-L. Ferri-Fioni, M. Fromant, A.-P. Bouin, C. Aubard, C. Lazennec, P. Plateau, and S. Blanquet Identification in Archaea of a Novel D-Tyr-tRNATyr Deacylase J. Biol. Chem., September 15, 2006; 281(37): 27575 - 27585. [Abstract] [Full Text] [PDF]

				D. Thompson and T. Simonson Molecular Dynamics Simulations Show That Bound Mg2+ Contributes to Amino Acid and Aminoacyl Adenylate Binding Specificity in Aspartyl-tRNA Synthetase through Long Range Electrostatic Interactions J. Biol. Chem., August 18, 2006; 281(33): 23792 - 23803. [Abstract] [Full Text] [PDF]

				B. Ruan and D. Soll The Bacterial YbaK Protein Is a Cys-tRNAPro and Cys-tRNACys Deacylase J. Biol. Chem., July 8, 2005; 280(27): 25887 - 25891. [Abstract] [Full Text] [PDF]

				O. Soutourina, J. Soutourina, S. Blanquet, and P. Plateau Formation of D-Tyrosyl-tRNATyr Accounts for the Toxicity of D-Tyrosine toward Escherichia coli J. Biol. Chem., October 8, 2004; 279(41): 42560 - 42565. [Abstract] [Full Text] [PDF]

				K. Kimura, L.-S. P. Tran, and Y. Itoh Roles and regulation of the glutamate racemase isogenes, racE and yrpC, in Bacillus subtilis Microbiology, September 1, 2004; 150(9): 2911 - 2920. [Abstract] [Full Text] [PDF]

				J. Broos, E. Gabellieri, E. Biemans-Oldehinkel, and G. B. Strambini Efficient biosynthetic incorporation of tryptophan and indole analogs in an integral membrane protein Protein Sci., September 1, 2003; 12(9): 1991 - 2000. [Abstract] [Full Text] [PDF]

				M. Fromant, M.-L. Ferri-Fioni, P. Plateau, and S. Blanquet Peptidyl-tRNA hydrolase from Sulfolobus solfataricus Nucleic Acids Res., June 15, 2003; 31(12): 3227 - 3235. [Abstract] [Full Text] [PDF]

				K. Lim, A. Tempczyk, N. Bonander, J. Toedt, A. Howard, E. Eisenstein, and O. Herzberg A Catalytic Mechanism for D-Tyr-tRNATyr Deacylase Based on the Crystal Structure of Hemophilus influenzae HI0670 J. Biol. Chem., April 4, 2003; 278(15): 13496 - 13502. [Abstract] [Full Text] [PDF]

				M.-L. Ferri-Fioni, E. Schmitt, J. Soutourina, P. Plateau, Y. Mechulam, and S. Blanquet Structure of Crystalline D-Tyr-tRNATyr Deacylase. A REPRESENTATIVE OF A NEW CLASS OF tRNA-DEPENDENT HYDROLASES J. Biol. Chem., December 7, 2001; 276(50): 47285 - 47290. [Abstract] [Full Text] [PDF]

				T. Uo, T. Yoshimura, N. Tanaka, K. Takegawa, and N. Esaki Functional Characterization of Alanine Racemase from Schizosaccharomyces pombe: a Eucaryotic Counterpart to Bacterial Alanine Racemase J. Bacteriol., April 1, 2001; 183(7): 2226 - 2233. [Abstract] [Full Text]

				J. Soutourina, S. Blanquet, and P. Plateau Role of D-Cysteine Desulfhydrase in the Adaptation of Escherichia coli to D-Cysteine J. Biol. Chem., October 26, 2001; 276(44): 40864 - 40872. [Abstract] [Full Text] [PDF]