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J Biol Chem, Vol. 273, Issue 45, 30003-30011, November 6, 1998

Purification and Characterization of MAR1
A MITOCHONDRIAL ASSOCIATED RIBONUCLEASE FROM LEISHMANIA TARENTOLAE

Juan D. Alfonzo, Otavio H. Thiemann^§, and Larry Simpson^§¶

From the  Howard Hughes Medical Institute, the ^§ Department of Molecular, Cell, and Developmental Biology, UCLA and the ^¶ Department of Medical Microbiology, Immunology, and Molecular Genetics, UCLA School of Medicine, Los Angeles, California 90095-1662

A relatively thermostable 22-kDa endoribonuclease (MAR1) was purified more than 10,000-fold from a mitochondrial extract of Leishmania tarentolae and the gene cloned. The purified nuclease has a K_m of 100-145 ± 33 nM and a V_max of 1.8-2.9 ± 2 nmol/min, depending on the RNA substrate, and yields a 3'-OH and a 5'-phosphate. Cleavage was limited to several specific sites in the substrate RNAs tested, but cleavage of pre-edited RNAs was generally independent of the addition of cognate guide RNA. The MAR1 gene was expressed in Escherichia coli or in L. tarentolae cells, and the recombinant protein was affinity-purified. The cleavage specificity of the recombinant enzyme from L. tarentolae was identical to that of the native enzyme. The single copy MAR1 gene maps to an 820-kilobase pair chromosome and contains an open reading frame of 579 nucleotides. The 18-amino acid N-terminal sequence shows characteristics of an uncleaved mitochondrial targeting sequence. Data base searching revealed two homologues of MAR1 corresponding to unidentified open reading frames in Caenorhabditis elegans (GenBank^TM accession number Z69637) and Archaeoglobus fulgidus (GenBank^TM accession number AE000943). The function of MAR1 in mitochondrial RNA metabolism in L. tarentolae remains to be determined.

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