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Originally published In Press as doi:10.1074/jbc.M409568200 on January 6, 2005

J. Biol. Chem., Vol. 280, Issue 12, 11352-11360, March 25, 2005
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Characterization and Purification of Saccharomyces cerevisiae RNase MRP Reveals a New Unique Protein Component*

Kelly Salinas{ddagger}, Sara Wierzbicki{ddagger}, Li Zhou, and Mark E. Schmitt§

From the Department of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, Syracuse, New York 13210

In the yeast Saccharomyces cerevisiae, RNase mitochondrial RNA processing (MRP) is an essential endoribonuclease that consists of one RNA component and at least nine protein components. Characterization of the complex is complicated by the fact that eight of the known protein components are shared with a related endoribonuclease, RNase P. To fully characterize the RNase MRP complex, we purified it to apparent homogeneity in a highly active state using tandem affinity purification. In addition to the nine known protein components, both Rpr2 and a protein encoded by the essential gene YLR145w were present in our preparations of RNase MRP. Precipitation of a tagged version of Ylr145w brought with it the RNase MRP RNA, but not the RNase P RNA. A temperature-sensitive ylr145w mutant was generated and found to exhibit a rRNA processing defect identical to that seen in other RNase MRP mutants, whereas no defect in tRNA processing was observed. Homologues of the Ylr145w protein were found in most yeasts, fungi, and Arabidopsis. Based on this evidence, we propose that YLR145w encodes a novel protein component of RNase MRP, but not RNase P. We recommend that this gene be designated RMP1, for RNase MRP protein 1.

Received for publication, August 19, 2004 , and in revised form, December 22, 2004.

* This work was supported by National Institutes of Health Grant GM064634 from the NIGMS. 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.

{ddagger} Both authors contributed equally to this work.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, 750 E. Adams St., Syracuse, NY 13210. Tel.: 315-464-8713; Fax: 315-464-8750; E-mail: schmittm{at}upstate.edu.


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