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J. Biol. Chem., Vol. 280, Issue 17, 16542-16545, April 29, 2005

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The RNase Z Homologue Encoded by Escherichia coli elaC Gene Is RNase BN^*

Benjamin Ezraty, Brian Dahlgren, and Murray P. Deutscher

From the Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101

In eukaryotes, archaea, and in some eubacteria, removal of 3' precursor sequences during maturation of tRNA is catalyzed by an endoribonuclease, termed RNase Z. In contrast, in Escherichia coli, a variety of exoribonucleases carry out final 3' maturation. Yet, E. coli retains an RNase Z homologue, ElaC, whose function is under active study. We have overexpressed and purified to homogeneity His-tagged ElaC and show here that it is, in fact, the previously described enzyme, RNase BN. Thus, purified ElaC displays structural and catalytic properties identical to those ascribed to RNase BN. In addition, an elaC mutant strain behaves identically to a known RNase BN^– strain, CAN. Finally, we show that wild type elaC can complement the mutation in strain CAN and that the elaC gene in strain CAN carries a nonsense mutation that results in loss of RNase BN activity. These data correct a previous misassignment for the gene encoding RNase BN. Based on the fact that the original RNase BN mutation has now been identified, we propose that the elaC gene be renamed rbn.

Received for publication, March 8, 2005

^* This work was supported by Grant GM16317 from the National Institutes of Health. 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. Tel.: 305-243-3150; Fax: 305-243-3955; E-mail: mdeutsch{at}med.miami.edu.

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