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J. Biol. Chem., Vol. 280, Issue 28, 26099-26104, July 15, 2005

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Association between Archaeal Prolyl- and Leucyl-tRNA Synthetases Enhances tRNA^Pro Aminoacylation^*

Mette Prætorius-Ibba, Theresa E. Rogers, Rachel Samson, Zvi Kelman, and Michael Ibba¶||

From the Department of Microbiology and ^¶Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210-1292 and the Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850

Aminoacyl-tRNA synthetase-containing complexes have been identified in different eukaryotes, and their existence has also been suggested in some Archaea. To investigate interactions involving aminoacyl-tRNA synthetases in Archaea, we undertook a yeast two-hybrid screen for interactions between Methanothermobacter thermautotrophicus proteins using prolyl-tRNA synthetase (ProRS) as the bait. Interacting proteins identified included components of methanogenesis, protein-modifying factors, and leucyl-tRNA synthetase (LeuRS). The association of ProRS with LeuRS was confirmed in vitro by native gel electrophoresis and size exclusion chromatography. Determination of the steady-state kinetics of tRNA^Pro charging showed that the catalytic efficiency (k_cat/K_m) of ProRS increased 5-fold in the complex with LeuRS compared with the free enzyme, whereas the K_m for proline was unchanged. No significant changes in the steady-state kinetics of LeuRS aminoacylation were observed upon the addition of ProRS. These findings indicate that ProRS and LeuRS associate in M. thermautotrophicus and suggest that this interaction contributes to translational fidelity by enhancing tRNA aminoacylation by ProRS.

Received for publication, March 31, 2005 , and in revised form, May 18, 2005.

^* This work was supported by National Institutes of Health Grant GM 65183 (to M. I.) and by National Science Foundation Grant MCB-0237483 (to Z. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Microbiology, The Ohio State University, 484 West 12th Ave., Columbus, OH 43210. Tel.: 614-292-2120; Fax: 614-292-8120; E-mail: ibba.1{at}osu.edu.

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