Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure

Nono Takeuchi, Makoto Kawakami, Akira Omori, Takuya Ueda, Linda L. Spremulli, Kimitsuna Watanabe*

*この研究の対応する著者

研究成果: Article査読

52 被引用数 (Scopus)

抄録

The mammalian mitochondrial methionyl-tRNA transformylase (MTF(mt)) was partially purified 2,200-fold from bovine liver mitochondria using column chromatography. The polypeptide responsible for MTF(mt) activity was excised from a sodium dodecyl sulfate-polyacrylamide gel and the amino acid sequences of several peptides were determined. The cDNA encoding bovine MTF(mt) was obtained and its nucleotide sequence was determined. The deduced amino acid sequence of the mature form of MTF(mt) consists of 357 amino acid residues. This sequence is about 30% identical to the corresponding Escherichia coli and yeast mitochondrial MTFs. Kinetic parameters governing the formylation of various tRNAs were obtained. Bovine MTF(mt) formylates its homologous mitochondrial methionyl-tRNA and the E. coli initiator methionyl-tRNA (Met- tRNA(fMet)) with essentially equal efficiency. The E. coli elongator methionyl-tRNA (Met-tRNA(mMet)) was also formylated although with somewhat less favorable kinetics. These results suggest that the substrate specificity of MTF(mt) is not as rigid as that of the E. coli MTF which clearly discriminates between the bacterial initiator and elongator Met-tRNAs. These observations are discussed in terms of the presence of a single tRNA(Met) gene in mammalian mitochondria.

本文言語English
ページ(範囲)15085-15090
ページ数6
ジャーナルJournal of Biological Chemistry
273
24
DOI
出版ステータスPublished - 1998 6月 12
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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