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J. Biol. Chem., Vol. 266, Issue 4, 2537-2541, Feb, 1991

Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase

W Zagorski, B Castaing, CJ Herbert, M Labouesse, R Martin and PP Slonimski
Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique associe a Universite Pierre et Maire Curie, Gif-sur- Yvette, France.

We have purified the product of the NAM2 gene, the mitochondrial leucyl- tRNA synthetase, from yeast mitochondria. The purified protein cross- reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the purified Escherichia coli leucyl-tRNA synthetase. The mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis is about 100 kDa, consistent with the size predicted by the gene sequence (102 kDa). The N-terminal sequence of the protein has been determined and shows that the first nine amino acids predicted by the gene sequence have been removed, probably during transport into the mitochondria.
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