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Papers In Press, published online ahead of print August 14, 2001
Integrated Biosciences, University of Tokyo, Chiba Prefecture 277-8562
Corresponding Author: t-suzuki{at}k.u-tokyo.ac.jp
The CCA-adding enzyme [ATP(CTP): tRNA nucleotidyltransferase (EC. 2.7.7.25)] generates the conserved CCA sequence responsible for the attachment of amino acid at the 3'-terminus of tRNA molecules. It was shown that enzymes from various organisms strictly recognize the elbow region of tRNA formed by D- and T-loops. However, most of mammalian mitochondrial (mt) tRNAs lack consensus sequences in both D- and T-loops. To characterize the mammalian mt CCA-adding enzymes, we have partially purified the enzyme from bovine liver mitochondria, and determined cDNA sequences from human and mouse dbESTs by mass spectrometric analysis. The identified sequences contained typical N-terminal peptides for mitochondrial protein import and had characteristics of the class II nucleotidyltransferase superfamily that includes eukaryotic and eubacterial CCA-adding enzymes. The human recombinant enzyme was overexpressed in E. coli and its CCA-adding activity was characterized using several mt tRNAs as substrates. The results clearly show that the human mt CCA-adding enzyme can efficiently repair mt tRNAs that are poor substrates for the E.coli enzyme, although both enzymes work equally well on cytoplasmic tRNAs. This suggests that the mammalian mt enzymes have evolved so as to recognize mt tRNAs with unusual structures.
J. Biol. Chem, 10.1074/jbc.M106202200
Submitted on July 3, 2001
Revised on August 14, 2001
Accepted on August 13, 2001
Identification and characterization of mammalian mitochondrial tRNA-nucleotidyltransferas
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