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J. Biol. Chem., Vol. 279, Issue 33, 34931-34937, August 13, 2004

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tRNA Recognition by Glutamyl-tRNA Reductase^*

Lennart Randau, Stefan Schauer, Alexandre Ambrogelly, Juan Carlos Salazar, Jürgen Moser, Shun-ichi Sekine¶, Shigeyuki Yokoyama¶, Dieter Söll||, and Dieter Jahn**

From the Institut für Mikrobiologie, Technical University Braunschweig, P. O. Box 3329, D-38023 Braunschweig, Germany, the Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, and the ^¶Cellular Signaling Laboratory and Structurome Group, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan

During the first step of porphyrin biosynthesis in Archaea, most bacteria, and in chloroplasts glutamyl-tRNA reductase (GluTR) catalyzes the NADPH-dependent reduction of glutamyl-tRNA to glutamate-1-semialdehyde. Elements in tRNA^Glu important for utilization by Escherichia coli GluTR were determined by kinetic analysis of 51 variant transcripts of E. coli Glu-tRNA^Glu. Base U8, the U13^*G22^**A46 base triple, the tertiary Watson-Crick base pair 19^*56, and the lack of residue 47 are required for GluTR recognition. All of these bases contribute to the formation of the unique tertiary core of E. coli tRNA-^Glu. Two tRNA^Glu molecules lacking the entire anticodon stem/loop but retaining the tertiary core structure remained substrates for GluTR, while further decreasing tRNA size toward a minihelix abolished GluTR activity. RNA footprinting experiments revealed the physical interaction of GluTR with the tertiary core of Glu-tRNA^Glu. E. coli GluTR showed clear selectivity against mischarged Glu-tRNA^Gln. We concluded that the unique tertiary core structure of E. coli tRNA^Glu was sufficient for E. coli GluTR to distinguish specifically its glutamyl-tRNA substrate.

Received for publication, February 11, 2004 , and in revised form, June 2, 2004.

^* This work was supported by grants from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie (to D. J.) and from the National Institute of General Medical Sciences and the Department of Energy (to D. S.). 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 may 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{at}trna.chem.yale.edu. ^** To whom correspondence may be addressed: Institute of Microbiology, Technical University Braunschweig, Spielmannstr 7, D-38106 Braunschweig, Germany. Tel.: 49-531-3915801; Fax: 49-531-3915854; E-mail: d.jahn{at}tu-bs.de.

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