The aminoacylation of structurally variant phenylalanine tRNAs from mitochondria and various nonmitochondrial sources by bovine mitochondrial phenylalanyl-tRNA synthetase.

@article{Kumazawa1989TheAO,
  title={The aminoacylation of structurally variant phenylalanine tRNAs from mitochondria and various nonmitochondrial sources by bovine mitochondrial phenylalanyl-tRNA synthetase.},
  author={Yoshio Kumazawa and Takashi Yokogawa and Etsuko Hasegawa and Kin-ichiro Miura and Kimitsuna Watanabe},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 22},
  pages={
          13005-11
        }
}
Bovine mitochondrial (mt) phenylalanine tRNA (tRNAPhe) was purified on a large scale using a new hybridization assay method developed by the authors. Although its melting profile suggested a loose higher order structure, presumably influenced by the apparent loss of D loop-T loop interaction necessary for forming a rigid L-shaped tertiary structure, its aminoacylation capacity catalyzed by mt phenylalanyl-tRNA synthetase (PheRS) was nearly equal to that of Escherichia coli tRNAPhe… CONTINUE READING

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Nucleic Thomas , P . 8 ( 1980 ) Prm

P. S. Thomas
  • . Natl . Acad . Sei . U . S . A
  • 1988