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Originally published In Press as doi:10.1074/jbc.M206929200 on July 18, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34749-34754, September 20, 2002
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Methanocaldococcus jannaschii Prolyl-tRNA Synthetase Charges tRNAPro with Cysteine*

Alexandre AmbrogellyDagger , Ivan AhelDagger , Carla PolycarpoDagger §, Shipra Bunjun-SrihariDagger , Bethany KrettDagger , Clarisse Jacquin-BeckerDagger , Benfang RuanDagger , Caroline Köhrer, Constantinos StathopoulosDagger , Uttam L. RajBhandary, and Dieter SöllDagger ||**

From the Departments of Dagger  Molecular Biophysics and Biochemistry and || Chemistry, Yale University, New Haven, Connecticut 06520-8114 and the  Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Methanocaldococcus jannaschii prolyl-tRNA synthetase (ProRS) was previously reported to also catalyze the synthesis of cysteinyl-tRNACys (Cys-tRNACys) to make up for the absence of the canonical cysteinyl-tRNA synthetase in this organism (Stathopoulos, C., Li, T., Longman, R., Vothknecht, U. C., Becker, H., Ibba, M., and Söll, D. (2000) Science 287, 479-482; Lipman, R. S., Sowers, K. R., and Hou, Y. M. (2000) Biochemistry 39, 7792-7798). Here we show by acid urea gel electrophoresis that pure heterologously expressed recombinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNAPro with cysteine. The enzyme is unable to aminoacylate purified mature M. jannaschii tRNACys with cysteine in contrast to facile aminoacylation of the same tRNA with cysteine by Methanococcus maripaludis cysteinyl-tRNA synthetase. Although M. jannaschii ProRS catalyzes the synthesis of Cys-tRNAPro readily, the enzyme is unable to edit this misaminoacylated tRNA. We discuss the implications of these results on the in vivo activity of the M. jannaschii ProRS and on the nature of the enzyme involved in the synthesis of Cys-tRNACys in M. jannaschii.

* This work was supported in part by the NIGMS, National Institutes of Health Grants GM22854 (to D. S.) and GM17151 (to U. L. R.), grants from the Department of Energy (to D. S.) and the National Aeronautics and Space Administration (to D. S.), and the U. S. Army Research Office Grant DAAD19-199-1-0300 (to U. L. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Predoctoral fellow of Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brazil).

** To whom correspondence should be addressed: Dept. of Molecular Biophysics and Biochemistry, Yale University, P. O. Box 208114, 266 Whitney Ave., New Haven, CT 06520-8114. Tel.: 203-432-6200; Fax: 203-432-6202; E-mail: soll@trna.chem.yale.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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