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J. Biol. Chem., Vol. 281, Issue 50, 38217-38225, December 15, 2006

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Trypanosoma Seryl-tRNA Synthetase Is a Metazoan-like Enzyme with High Affinity for tRNA^Sec*

Renaud Geslain¹, Eric Aeby¹, Tanit Guitart, Thomas E. Jones, Manuel Castro de Moura, Fabien Charrière, André Schneider, and Lluís Ribas de Pouplana^¶2

From the ^¶Institució Catalana de Recerca i Estudis Avançats (ICREA) and Institute for Research in Biomedicine, Barcelona, Barcelona Science Park, C/Samitier 1-5, Barcelona 08015, Catalonia, Spain and the Department of Biology/Cell & Developmental Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland

Trypanosomatids are important human pathogens that form a basal branch of eukaryotes. Their evolutionary history is still unclear as are many aspects of their molecular biology. Here we characterize essential components required for the incorporation of serine and selenocysteine into the proteome of Trypanosoma. First, the biological function of a putative Trypanosoma seryl-tRNA synthetase was characterized in vivo. Secondly, the molecular recognition by Trypanosoma seryl-tRNA synthetase of its cognate tRNAs was dissected in vitro. The cellular distribution of tRNA^Sec was studied, and the catalytic constants of its aminoacylation were determined. These were found to be markedly different from those reported in other organisms, indicating that this reaction is particularly efficient in trypanosomatids. Our functional data were analyzed in the context of a new phylogenetic analysis of eukaryotic seryl-tRNA synthetases that includes Trypanosoma and Leishmania sequences. Our results show that trypanosomatid seryl-tRNA synthetases are functionally and evolutionarily more closely related to their metazoan homologous enzymes than to other eukaryotic enzymes. This conclusion is supported by sequence synapomorphies that clearly connect metazoan and trypanosomatid seryl-tRNA synthetases.

Received for publication, August 16, 2006 , and in revised form, September 28, 2006.

^* This work was supported by Grants BIO2003-02611 from the Spanish Ministry of Science and Education, and 3100-067906 of the Swiss National Foundation (to A. S.), a Marie Curie International Reintegration Fellowship (to L. R. P.), and a Fellowship of the Novartis Foundation (F. C.). 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.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 34-934-034868; Fax: 34-934-034870; E-mail: lluisribas{at}pcb.ub.es.

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