The processing of human mitochondrial leucyl‐tRNA synthetase in the insect cells

摘要

>A His-tagged full-length cDNA of human mitochondrial leucyl-tRNA synthetase was expressed in a baculovirus system. The N-terminal sequence of the enzyme isolated from the mitochondria of insect cells was found to be IYSATGKWTKEYTL, indicating that the mitochondrial targeting signal peptide was cleaved between Ser39 and Ile40 after the enzyme precursor was translocated into mitochondria. The enzyme purified from mitochondria catalyzed the leucylation of Escherichia coli tRNA₁ Leu(CAG) and Aquifex aeolicus tRNALeu(GAG) with higher catalytic activity in the leucylation of E. coli tRNALeu than that previously expressed in E. coli without the N-terminal 21 residues.