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Originally published In Press as doi:10.1074/jbc.M208717200 on September 30, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46145-46150, November 29, 2002
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Dehydrogenases from All Three Domains of Life Cleave RNA*

Elena Evguenieva-HackenbergDagger §, Emile Schiltz, and Gabriele KlugDagger

From the Dagger  Institut für Mikrobiologie und Molekularbiologie der Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany and the  Institut für Organische Chemie und Biochemie der Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany

Specific interactions of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with RNA have been reported both in vitro and in vivo. We show that eukaryotic and bacterial GAPDH and two proteins from the hyperthermophilic archaeon Sulfolobus solfataricus, which are annotated as dehydrogenases, cleave RNA producing similar degradation patterns. RNA cleavage is most efficient at 60 °C, at MgCl2 concentrations up to 5 mM, and takes place between pyrimidine and adenosine. The RNase active center of the putative aspartate semialdehyde dehydrogenase from S. solfataricus is located within the N-terminal 73 amino acids, which comprise the first mononucleotide-binding site of the predicted Rossmann fold. Thus, RNA cleavage has to be taken into account in the ongoing discussion of the possible biological function of RNA binding by dehydrogenases.

* This work was supported by the Deutsche Forschungsgemeinschaft (Kl 563/11-1), and the Fonds der Chemischen Industrie.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.

§ To whom correspondence should be addressed. Tel.: 49-641-99-35550/57; Fax: 49-641-99-35549; E-mail: Elena.Evguenieva-Hackenberg@mikro.bio.uni-giessen.de.

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