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The mitochondrial and cytoplasmic valyl transfer rna synthetases in tetrahymena pyriformis are indistinguishable


Archives of Biochemistry and Biophysics 191(2): 437-443
The mitochondrial and cytoplasmic valyl transfer rna synthetases in tetrahymena pyriformis are indistinguishable
The mitochondrial and cytoplasmic valyl tRNA synthetases from T. pyriformis cannot be differentiated through hydroxylapatite, DEAE-cellulose or phosphocellulose column chromatography. Both enzymes show the same mean sedimentation coefficient of 5.9 S in sucrose gradient centrifugation analysis; when bound with tRNA, they are relatively stable and sediment at 7.8 S. The temperature optimum for aminoacylation reaction is 27.5.degree. C, the optimum Mg2+ concentration is 4.4 mM, and substrate affinities (Km values) for valine and ATP in aminoacylation are the same for both enzymes at 1.0 .mu.M, and 2.5 .mu.M, respectively. These enzymes show identical specificities for acylation of different tRNA species, i.e., Tetrahymena and rat liver tRNA can be equally well recognized, but no significant acylation can be observed with Escherichia coli and Saccharomyces tRNA. Probably, the mitochondrial and cytoplasmic valyl tRNA synthetases in T. pyriformis are identical.


Accession: 006719055



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The mitochondrial and cytoplasmic valyl tRNA synthetases in Tetrahymena are indistinguishable. Archives of Biochemistry and Biophysics 191(2): 437-443, 1978

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